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1FH9

CRYSTAL STRUCTURE OF THE XYLANASE CEX WITH XYLOBIOSE-DERIVED LACTAM OXIME INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVrITELDI
ChainResidueDetails
AGLY226-ILE236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:7918478
ChainResidueDetails
AGLU127

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:1678739
ChainResidueDetails
AGLU233

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU127
AGLU233
AASP235
AHIS205

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU127

site_idMCSA1
Number of Residues5
DetailsM-CSA 548
ChainResidueDetails
AGLU127proton acceptor, proton donor
AASN169electrostatic stabiliser
AHIS205electrostatic stabiliser
AGLU233electrostatic stabiliser, nucleofuge, nucleophile
AASP235electrostatic stabiliser

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PDB entries from 2024-11-06

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