Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RW3

Crystal Structure of Agd31B, alpha-transglucosylase, complexed with a non-covalent 1,2- Cyclophellitol aziridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0030246molecular_functioncarbohydrate binding
C0003824molecular_functioncatalytic activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0030246molecular_functioncarbohydrate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23132856
ChainResidueDetails
CASP412
AASP412
BASP412

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P31434
ChainResidueDetails
CGLU415
AGLU415
BGLU415

site_idSWS_FT_FI3
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P31434
ChainResidueDetails
CASP480
AASP480
BASP480

site_idSWS_FT_FI4
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:23132856
ChainResidueDetails
CASP299
AHIS540
BASP299
BGLU417
BARG463
BASP480
BHIS540
CGLU417
CARG463
CASP480
CHIS540
AASP299
AGLU417
AARG463
AASP480

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon