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4FNR

Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033531biological_processstachyose metabolic process
A0034484biological_processraffinose catabolic process
A0051289biological_processprotein homotetramerization
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004557molecular_functionalpha-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0016052biological_processcarbohydrate catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033531biological_processstachyose metabolic process
B0034484biological_processraffinose catabolic process
B0051289biological_processprotein homotetramerization
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004557molecular_functionalpha-galactosidase activity
C0005975biological_processcarbohydrate metabolic process
C0016052biological_processcarbohydrate catabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033531biological_processstachyose metabolic process
C0034484biological_processraffinose catabolic process
C0051289biological_processprotein homotetramerization
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004557molecular_functionalpha-galactosidase activity
D0005975biological_processcarbohydrate metabolic process
D0016052biological_processcarbohydrate catabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033531biological_processstachyose metabolic process
D0034484biological_processraffinose catabolic process
D0051289biological_processprotein homotetramerization
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues16
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GIelVvLDDg.Wfge....RD
ChainResidueDetails
AGLY359-ASP374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23012371
ChainResidueDetails
AASP478
BASP478
CASP478
DASP478

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:23012371
ChainResidueDetails
AASP548
BASP548
CASP548
DASP548

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:23012371, ECO:0007744|PDB:4FNT
ChainResidueDetails
AASP53
BASP366
BARG443
BLYS476
BCYS526
BASP548
CASP53
CTRP199
CASP366
CARG443
CLYS476
ATRP199
CCYS526
CASP548
DASP53
DTRP199
DASP366
DARG443
DLYS476
DCYS526
DASP548
AASP366
AARG443
ALYS476
ACYS526
AASP548
BASP53
BTRP199

220113

PDB entries from 2024-05-22

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