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6MVG

Crystal structure of FMN-binding beta-glucuronidase from Ruminococcus gnavus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue FMN A 801
ChainResidue
AASP156
ATYR159
AGLY164
ALYS166
APHE183
ALYS359
ATYR366
AMET404

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 802
ChainResidue
AASP44
AGLY45
AASP48
AASP521
AASP41

site_idAC3
Number of Residues6
Detailsbinding site for residue FMN B 801
ChainResidue
BASP156
BTYR159
BPHE183
BLYS359
BTYR366
BMET404

site_idAC4
Number of Residues5
Detailsbinding site for residue CA B 802
ChainResidue
BASP41
BASP44
BGLY45
BASP48
BASP521

site_idAC5
Number of Residues6
Detailsbinding site for residue FMN C 801
ChainResidue
CASP156
CTYR159
CPHE183
CLYS359
CTYR366
CMET404

site_idAC6
Number of Residues5
Detailsbinding site for residue CA C 802
ChainResidue
CASP41
CASP44
CGLY45
CASP48
CASP521

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PDB entries from 2024-07-31

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