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1BF2

STRUCTURE OF PSEUDOMONAS ISOAMYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019156molecular_functionisoamylase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 751
ChainResidue
AASP128
AGLU229
ATHR230
AASN232
AASP259
AHOH1002

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP375

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU435

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2
ChainResidueDetails
AASP128
AGLU229
ATHR230
AASN232
AASP259

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP510

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9719642, 12196524
ChainResidueDetails
AASP510
AASP375
AGLU435

site_idMCSA1
Number of Residues8
DetailsM-CSA 421
ChainResidueDetails
AASP128metal ligand
AGLU229metal ligand
ATHR230metal ligand
AASN232metal ligand
AASP259metal ligand
AASP375covalent catalysis
AGLU435proton shuttle (general acid/base)
AASP510transition state stabiliser

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PDB entries from 2024-09-11

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