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6K9O

Crystal Structure Analysis of Protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue GOL A 201
ChainResidue
AVAL46
AHOH341
AHOH378
AHOH420
AGLU86
ATYR88
AGLU177
AHOH301
AHOH309
AHOH314
AHOH321
AHOH339

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD A 202
ChainResidue
AASN82
ASER146

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 203
ChainResidue
AASN82
ASER146

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF
ChainResidueDetails
APRO83-PHE93

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA
ChainResidueDetails
AVAL174-ALA185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLU86

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLU177

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24419374
ChainResidueDetails
ATYR73
ATYR77
ATYR88
AARG122
APRO126
AGLN136
ATYR171

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN38
AASN61

226707

PDB entries from 2024-10-30

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