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3EZ8

Crystal Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 538
ChainResidue
AASP302
AGLU304
AASP307
AGLU308
AALA344
AHOH544

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 539
ChainResidue
AHOH636
AHOH858
AHOH921
AHOH922
ASER465
AASP468
AVAL470

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 540
ChainResidue
ACYS104
ACYS121
AHIS122
AHIS142

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 541
ChainResidue
APRO33
AARG37
ATHR73

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 542
ChainResidue
ATRP339
AGLU377
ALEU381
AARG410
AHOH627

Functional Information from PROSITE/UniProt
site_idPS00592
Number of Residues27
DetailsGH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YLFGaNplgqCYVTGf....GqrPVrhPHHR
ChainResidueDetails
ATYR437-ARG463

site_idPS00698
Number of Residues19
DetailsGH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YiDhqdsYstnEvAvywNS
ChainResidueDetails
ATYR504-SER522

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1js4
ChainResidueDetails
AASP143
AGLU515
AASP146

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PDB entries from 2024-07-24

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