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4LGX

Structure of Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ATYR28
AASP151
AGLU153
AMET220
ATYR222
AGOL503
AHOH1164

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ATHR69
AASN70
AGLY115
AARG117
AHOH666
AHOH680
AHOH790
AHOH799
AHOH1029
AGLN67
AGLU68

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AASP34
ATHR36
AMET220
ATYR222
AASP223
ATYR276
AARG278
ATRP395
AACT501
AHOH1160
AHOH1165

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. LDGIDLDwE
ChainResidueDetails
ALEU145-GLU153

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PDB entries from 2024-07-24

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