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4QQS

Crystal structure of a thermostable family-43 glycoside hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EPE A 401
ChainResidue
AASP17
AHOH579
AHOH875
AHOH1011
ATRP72
AALA73
AILE125
AASP126
AGLU195
ATYR215
AHIS256
AHOH557

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AGLU75
AHIS256
AHOH523
AHOH577
AHOH582
AHOH707

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EPE A 403
ChainResidue
AASP279
AHOH671
BTYR237
BSER238
BSER280
BHOH595
BHOH807

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EPE B 401
ChainResidue
ALYS245
AARG246
AMET247
BASP17
BTRP72
BTYR215
BARG285
BHOH583
BHOH816
BHOH838
BHOH840
BHOH880

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 402
ChainResidue
BGLU75
BHIS256
BHOH550
BHOH586
BHOH598
BHOH1021

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PDB entries from 2024-07-31

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