Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1REF

ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 2,3-EPOXYPROPYL-BETA-D-XYLOSIDE

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
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
ATYR87
BTYR87

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLY178
BGLY178

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24419374
ChainResidueDetails
ALEU74
BILE89
BVAL123
BSER127
BTYR137
BGLN172
AGLY78
AILE89
AVAL123
ASER127
ATYR137
AGLN172
BLEU74
BGLY78

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATRP39
APHE62
BTRP39
BPHE62

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU177
AGLU86

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
BGLU177
BGLU86

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon