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Calcium in PDB 1hmw: Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis

Enzymatic activity of Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis

All present enzymatic activity of Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis:
4.2.2.5;

Protein crystallography data

The structure of Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis, PDB code: 1hmw was solved by W.Huang, L.Boju, L.Tkalec, H.Su, H.O.Yang, N.S.Gunay, R.J.Linhardt, Y.S.Kim, A.Matte, M.Cygler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.900, 86.900, 192.300, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 27.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis (pdb code 1hmw). 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 Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis, PDB code: 1hmw:

Calcium binding site 1 out of 1 in 1hmw

Go back to Calcium Binding Sites List in 1hmw
Calcium binding site 1 out of 1 in the Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Active Site of Chondroitinase Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1801

b:28.9
occ:1.00
 OD1 A:ASP416 2.3 35.9 1.0
OD2 A:ASP407 2.3 34.4 1.0
O A:HOH829 2.3 24.2 1.0
O A:TYR417 2.4 36.4 1.0
OE2 A:GLU405 2.5 35.8 1.0
O A:HOH979 2.5 34.9 1.0
OD1 A:ASP407 2.6 34.9 1.0
CG A:ASP407 2.8 34.5 1.0
CD A:GLU405 3.5 35.3 1.0
CG A:ASP416 3.5 35.2 1.0
C A:TYR417 3.6 39.1 1.0
N A:TYR417 3.8 35.3 1.0
CG A:GLU405 3.8 31.8 1.0
NZ A:LYS408 3.8 34.1 1.0
C A:ASP416 4.1 33.7 1.0
CA A:ASP416 4.2 34.2 1.0
OD2 A:ASP416 4.3 33.3 1.0
CA A:TYR417 4.3 38.0 1.0
CB A:ASP407 4.3 33.3 1.0
O A:LEU418 4.4 40.6 1.0
O A:HOH802 4.4 31.2 1.0
CB A:ASP416 4.5 33.3 1.0
O A:HOH967 4.5 42.1 1.0
C A:LEU418 4.6 40.4 1.0
OE1 A:GLU405 4.6 35.9 1.0
N A:LEU418 4.6 41.4 1.0
OD1 A:ASP420 4.7 36.7 1.0
O A:ASP416 4.7 33.3 1.0
CA A:LEU418 4.8 40.8 1.0
O A:HOH971 4.9 55.1 1.0
CB A:TYR417 5.0 38.7 1.0

Reference:

W.Huang, L.Boju, L.Tkalec, H.Su, H.O.Yang, N.S.Gunay, R.J.Linhardt, Y.S.Kim, A.Matte, M.Cygler. Active Site of Chondroitin Ac Lyase Revealed By the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis. Biochemistry V. 40 2359 2001.
ISSN: ISSN 0006-2960
PubMed: 11327856
DOI: 10.1021/BI0024254
Page generated: Mon Jul 7 15:39:41 2025

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