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Calcium in PDB 1fls: Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor

Other elements in 1fls:

The structure of Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor (pdb code 1fls). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor, PDB code: 1fls:

Calcium binding site 1 out of 1 in 1fls

Go back to Calcium Binding Sites List in 1fls
Calcium binding site 1 out of 1 in the Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca168

b:0.2
occ:1.00
O A:LEU81 2.9 0.2 1.0
O A:GLY77 2.9 0.4 1.0
O A:SER79 2.9 0.2 1.0
OD1 A:ASP76 3.0 0.3 1.0
OE2 A:GLU102 3.0 0.9 1.0
OD2 A:ASP99 3.0 0.3 1.0
O A:PRO78 3.0 0.3 1.0
H A:LEU81 3.2 0.2 1.0
N A:LEU81 3.3 0.2 1.0
C A:SER79 3.3 0.3 1.0
HA3 A:GLY80 3.4 0.3 1.0
C A:GLY80 3.5 0.2 1.0
C A:LEU81 3.5 0.2 1.0
HB3 A:PHE75 3.5 0.4 1.0
C A:PRO78 3.6 0.3 1.0
N A:GLY80 3.6 0.3 1.0
HD23 A:LEU82 3.6 1.0 1.0
CA A:GLY80 3.7 0.3 1.0
H A:ASP76 3.7 0.3 1.0
HD1 A:PHE75 3.8 0.5 1.0
C A:GLY77 3.9 0.3 1.0
CA A:LEU81 3.9 0.2 1.0
HA A:LEU82 4.0 0.2 1.0
HB2 A:LEU81 4.0 0.3 1.0
O A:GLY80 4.1 0.2 1.0
N A:SER79 4.1 0.3 1.0
CA A:SER79 4.1 0.3 1.0
CD A:GLU102 4.1 0.8 1.0
CG A:ASP76 4.1 0.4 1.0
CG A:ASP99 4.2 0.4 1.0
H A:GLY77 4.3 0.4 1.0
HA A:SER79 4.3 0.3 1.0
H A:GLY80 4.3 0.4 1.0
N A:LEU82 4.3 0.2 1.0
N A:ASP76 4.4 0.4 1.0
CA A:PRO78 4.4 0.4 1.0
N A:GLY77 4.5 0.3 1.0
HA A:PRO78 4.5 0.4 1.0
CB A:LEU81 4.5 0.2 1.0
CB A:PHE75 4.5 0.4 1.0
HG3 A:GLU102 4.6 1.2 1.0
N A:PRO78 4.6 0.3 1.0
CD1 A:PHE75 4.6 0.4 1.0
CA A:LEU82 4.7 0.2 1.0
CD2 A:LEU82 4.7 0.2 1.0
HG2 A:GLU102 4.7 1.0 1.0
OD2 A:ASP76 4.7 0.5 1.0
HA2 A:GLY80 4.7 0.4 1.0
CG A:GLU102 4.7 0.5 1.0
HB3 A:ASP99 4.8 0.3 1.0
HA A:LEU81 4.9 0.2 1.0
CA A:GLY77 4.9 0.4 1.0
H A:SER79 4.9 0.3 1.0
C A:ASP76 4.9 0.4 1.0
HB3 A:LEU81 4.9 0.2 1.0
CB A:ASP99 5.0 0.2 1.0
HB2 A:ASP99 5.0 0.3 1.0
H A:LEU82 5.0 0.2 1.0

Reference:

F.J.Moy, P.K.Chanda, J.M.Chen, S.Cosmi, W.Edris, J.I.Levin, R.Powers. High-Resolution Solution Structure of the Catalytic Fragment of Human Collagenase-3 (Mmp-13) Complexed with A Hydroxamic Acid Inhibitor. J.Mol.Biol. V. 302 671 2000.
ISSN: ISSN 0022-2836
PubMed: 10986126
DOI: 10.1006/JMBI.2000.4082
Page generated: Thu Jul 11 08:14:20 2024

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