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Calcium in PDB 3k7l: Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins

Protein crystallography data

The structure of Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins, PDB code: 3k7l was solved by H.H.Guan, W.G.Wu, C.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.650, 91.650, 124.235, 90.00, 90.00, 90.00
R / Rfree (%) 22.4 / 23.4

Other elements in 3k7l:

The structure of Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins (pdb code 3k7l). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins, PDB code: 3k7l:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 3k7l

Go back to Calcium Binding Sites List in 3k7l
Calcium binding site 1 out of 3 in the Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca701

b:57.8
occ:1.00
OE1 A:GLU208 2.3 54.5 1.0
OD1 A:ASN398 2.4 60.4 1.0
O A:CYS395 2.5 43.7 1.0
OD1 A:ASP292 2.7 34.4 1.0
OD2 A:ASP292 2.8 30.1 1.0
CG A:ASP292 3.1 36.5 1.0
CG A:ASN398 3.3 53.9 1.0
C A:CYS395 3.3 41.9 1.0
CD A:GLU208 3.5 50.9 1.0
CB A:CYS395 3.6 46.4 1.0
ND2 A:ASN398 3.6 53.5 1.0
CA A:CYS395 3.8 41.0 1.0
CG A:GLU208 4.1 41.3 1.0
O A:ASN398 4.4 38.9 1.0
SG A:CYS395 4.4 49.8 1.0
N A:ILE396 4.4 34.8 1.0
OE2 A:GLU208 4.5 50.0 1.0
CB A:ASP292 4.6 35.5 1.0
CB A:ASN398 4.7 50.7 1.0
CA A:ILE396 4.7 32.0 1.0
O A:TYR206 4.7 39.3 1.0
N A:ASN398 4.7 41.4 1.0
CB A:GLU208 4.9 35.0 1.0

Calcium binding site 2 out of 3 in 3k7l

Go back to Calcium Binding Sites List in 3k7l
Calcium binding site 2 out of 3 in the Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca702

b:45.2
occ:1.00
OD2 A:ASP489 2.2 44.6 1.0
OD2 A:ASP474 2.3 41.4 1.0
O A:LEU475 2.4 45.8 1.0
OE1 A:GLU477 2.5 38.7 1.0
O A:VAL490 2.6 44.3 1.0
OE2 A:GLU477 2.8 47.5 1.0
CD A:GLU477 3.0 41.7 1.0
CG A:ASP474 3.4 41.0 1.0
CG A:ASP489 3.4 45.8 1.0
C A:LEU475 3.5 47.1 1.0
N A:VAL490 3.6 45.0 1.0
C A:VAL490 3.7 42.9 1.0
OD1 A:ASP474 3.8 41.6 1.0
N A:LEU475 4.0 47.5 1.0
CA A:ASP489 4.1 41.8 1.0
C A:ASP489 4.2 42.5 1.0
OD1 A:ASP489 4.3 45.9 1.0
CA A:VAL490 4.3 43.0 1.0
CA A:LEU475 4.3 47.3 1.0
CB A:ASP489 4.4 44.9 1.0
N A:PRO476 4.5 46.4 1.0
CG A:GLU477 4.5 38.1 1.0
CB A:LEU475 4.6 41.8 1.0
CB A:ASP474 4.6 43.8 1.0
CA A:PRO476 4.6 46.6 1.0
CD A:ARG467 4.6 35.0 1.0
C A:PRO476 4.6 45.6 1.0
N A:GLU477 4.7 36.6 1.0
CD2 A:PHE491 4.7 25.3 1.0
C A:ASP474 4.8 48.5 1.0
N A:PHE491 4.8 42.1 1.0
CA A:ASP474 4.8 47.7 1.0
CA A:PHE491 4.9 40.7 1.0

Calcium binding site 3 out of 3 in 3k7l

Go back to Calcium Binding Sites List in 3k7l
Calcium binding site 3 out of 3 in the Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca703

b:34.5
occ:1.00
O A:ILE410 2.3 45.0 1.0
ND2 A:ASN413 2.3 28.1 1.0
OE1 A:GLU417 2.3 37.0 1.0
O A:PHE415 2.4 28.7 1.0
OD2 A:ASP423 2.4 40.8 1.0
OE1 A:GLU420 2.6 38.6 1.0
OE2 A:GLU420 2.6 39.1 1.0
CD A:GLU420 3.0 35.2 1.0
CG A:ASN413 3.3 30.7 1.0
CD A:GLU417 3.3 36.4 1.0
CG A:ASP423 3.4 40.8 1.0
C A:ILE410 3.4 46.6 1.0
C A:PHE415 3.6 29.9 1.0
OD1 A:ASN413 3.6 23.2 1.0
CB A:ASP423 3.9 41.1 1.0
OE2 A:GLU417 4.0 38.3 1.0
N A:PHE415 4.0 28.6 1.0
N A:GLU417 4.1 29.7 1.0
N A:ASN413 4.1 33.3 1.0
CA A:CYS411 4.1 41.3 1.0
N A:CYS411 4.2 41.2 1.0
N A:GLY412 4.2 36.8 1.0
N A:ILE410 4.2 45.1 1.0
CG A:GLU417 4.3 33.3 1.0
OD1 A:ASP423 4.4 42.5 1.0
CA A:PHE415 4.4 29.8 1.0
CA A:ILE410 4.4 44.9 1.0
CB A:GLU417 4.4 33.3 1.0
CB A:ASN413 4.5 31.1 1.0
N A:VAL416 4.5 34.4 1.0
CA A:VAL416 4.5 33.3 1.0
CG A:GLU420 4.5 33.2 1.0
C A:VAL416 4.7 32.3 1.0
CA A:ASN413 4.7 31.7 1.0
C A:CYS411 4.7 40.5 1.0
C A:ASN413 4.7 32.2 1.0
N A:TYR414 4.7 32.9 1.0
O A:HOH725 4.8 39.2 1.0
CB A:PHE415 4.9 34.7 1.0
CA A:GLU417 4.9 31.4 1.0

Reference:

H.H.Guan, K.S.Goh, F.Davamani, P.L.Wu, Y.W.Huang, J.Jeyakanthan, W.G.Wu, C.J.Chen. Structures of Two Elapid Snake Venom Metalloproteases with Distinct Activities Highlight the Disulfide Patterns in the D Domain of Adamalysin Family Proteins J.Struct.Biol. V. 169 294 2010.
ISSN: ISSN 1047-8477
PubMed: 19932752
DOI: 10.1016/J.JSB.2009.11.009
Page generated: Sat Jul 13 12:05:45 2024

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