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

4XV0

Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Trichoderma reesei

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 Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
AGLY70
AARG191
AHOH505
AHOH520
AHOH532
AHOH621
AHOH629

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH505
AHOH507
AHOH517
AHOH519
AHOH856
AARG74
AHOH504

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 403
ChainResidue
AILE143
AASN144
AASN145
ATHR148
AHOH824
AHOH865

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 404
ChainResidue
AGLN97
ATRP108
AGLN135
AARG163
AHOH509
AHOH523

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG150
AHOH616
AHOH758

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 406
ChainResidue
AGLN103
AHOH878

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 407
ChainResidue
AGLN53
AARG57

site_idAC8
Number of Residues1
Detailsbinding site for residue CL A 408
ChainResidue
AARG213

site_idAC9
Number of Residues2
Detailsbinding site for residue CL A 409
ChainResidue
AGLU75
AHOH683

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 410
ChainResidue
ALYS60
ASER304
AASN332
AHOH514
AHOH515
AHOH540

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL A 411
ChainResidue
ASER199
AARG203
AGLN242
AVAL244
AHOH501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01096
ChainResidueDetails
AGLU176

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01096
ChainResidueDetails
AGLU282

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:Q9P973
ChainResidueDetails
APCA46

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon