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

1TE1

Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004568molecular_functionchitinase activity
A0004857molecular_functionenzyme inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006952biological_processdefense response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0050832biological_processdefense response to fungus
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. PLvEYYILEsY
ChainResidueDetails
BPRO82-TYR92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062
ChainResidueDetails
BGLU85

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
BGLU176
AASN265

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Interaction with protein inhibitor XIP-I => ECO:0000269|PubMed:15181003
ChainResidueDetails
BASN10
BTYR136
BGLU142

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
BGLU85
BGLU176

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon