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1X6N

Crystal structure of S. marcescens chitinase A mutant W167A in complex with allosamidin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AO3 A 564
ChainResidue
ATYR163
ATYR444
AARG446
AGLU473
AILE476
ATRP539
AGLU540
AHOH728
APHE191
ATRP275
ATHR276
AASP313
AGLU315
AMET388
ATYR390
AASP391

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE
ChainResidueDetails
APHE307-GLU315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU315

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP313
AGLU315
ATYR390

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP313
AGLU315

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP311
AGLU315

site_idMCSA1
Number of Residues4
DetailsM-CSA 478
ChainResidueDetails
AASP311electrostatic stabiliser
AASP313steric role
AGLU315proton shuttle (general acid/base)
ATYR390electrostatic destabiliser

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PDB entries from 2024-07-10

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