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3NQH

Crystal structure of a glycosyl hydrolase (BT_2959) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 2.11 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AGLU105
AHOH701
AARG106
ATYR129
AASP163
AGLU207
AGLN262
AHOH512
AHOH588
AHOH670

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AGLN93
ASER94
ALYS358

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
AASP439
ALYS440

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PDB entries from 2025-06-18

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