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5JRM

Crystal Structure of a Xylanase at 1.56 Angstroem resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
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 Residues4
Detailsbinding site for residue GOL A 201
ChainResidue
ATYR76
APRO125
ASER126
AHOH302

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 202
ChainResidue
AHOH355
AHOH386
AHOH401
ATHR21
AASN23
AGLN102
AHOH312
AHOH337

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 203
ChainResidue
AVAL107
AASN108
AHOH400

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 204
ChainResidue
AARG144
ASER145
ASER146
AHOH320
AHOH331
AHOH339

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF
ChainResidueDetails
APRO82-PHE92

229380

PDB entries from 2024-12-25

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