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3USZ

Crystal structure of truncated exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1

Replaces:  3F94
Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 901
ChainResidue
AGLU179
ALEU592
AASN593
AHOH887
AHOH919
AHOH1085

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
AILE100
AHOH939
AHOH1230
AALA92
AASP94
AASP98

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 903
ChainResidue
ALYS298
AVAL300
ACYS303

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 824
ChainResidue
AHOH1155

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 825
ChainResidue
AASN7
AARG239
ALYS334

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLKnQlgfdGFVVSDwnA
ChainResidueDetails
AVAL279-ALA296

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PDB entries from 2024-08-14

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