Structure of PDB 5m6g Chain A

Receptor sequence

>5m6gA (length=579) Species: 1382595 (Saccharopolyspora erythraea D)

RPAYRDPRLPVPDRVDDLMARMSLDDKLGQMVQVERKAAGPQAVADHRIG
SVLSGGGSAPEPNTPQAWADMYDSYQRAALSTPLGIPLIYGVDAVHGHNN
VHGATIYPHNIGLGATGNPDLVQRIGAATAEEVAATGIDWSFAPCVCVAR
DDRWGRTYESFGEKSENASAMTSAVTGLQGEALGATPSSVMATAKHYVGD
GGTTGGDDQGNTEISEQELREIHLPPFREAIARGVGSVMVSYSSWNGEKL
HASTYLVNDVLKGELGFTGLVVSDYDAIDKLDGQEDFTPDEVRASVNAGI
DMFMMSSRHEKFIDYLRAEVEAGRVPAERIDDANRRILTKKFELGLFERP
FAQRDLLPTVGSAEHRELARQAVRESQVLLRNDGVLPLAKDGGKLFVAGK
NADDIGNQSGGWTISWQGSSGDITEGTTILEGIRAAASGSEVTYDRHGNG
VDGSYRAAIAVVGETPYAEFEGDRPGGLGLDEEDRATIAKLRASGVPVVV
VTVSGRPLDIAGEVDGWNALLASWLPGSEGQGVADVLFGDHNPTGKLPMT
WMRSFDQLPINDGDGQDPLFPHGFGLSYG

3D structure

• PDB: 5m6g Crystal structure Glucan 1,4-beta-glucosidase from Saccharopolyspora erythraea
• Chain: A
• Resolution: 1.829 Å

Enzymatic activity

• Enzyme Commision number: 3.2.1.21: beta-glucosidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	A	D315 D318 Q320 D322 E327	D279 D282 Q284 D286 E291
BS02	MG	A	D243 D509	D207 D473
BS03	MG	A	E199 I596 N597	E163 I560 N561
BS04	MG	A	E167 H401	E131 H365
BS05	MG	A	G173 D175	G137 D139
BS06	SOR	A	G91 G92 D129 R192 K231 H232 D310 W448	G55 G56 D93 R156 K195 H196 D274 W412

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0008422 beta-glucosidase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0031217 glucan 1,4-beta-glucosidase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0009251 glucan catabolic process

External links

• PDB: RCSB:5m6g, PDBe:5m6g, PDBj:5m6g
• PDBsum: 5m6g
• UniProt: A4FNP6