Structure of PDB 6rjm Chain A

Receptor sequence
>6rjmA (length=453) Species: 1453998 (Agrobacterium tumefaciens A6) [Search protein sequence]
YPMTDHKALAARFPGDFLFGVATASFQIEGATKVDGRKPSIWDAFCNMPG
HVFGRHNGDVACDHYNRWEDDLDLIKEMGVEAYRFSIAWPRIIPDGFGPI
NEKGLDFYDRLVDGCKARGIKTYATLYHWDLPLTLMGDGGWASRSTAHAF
QRYAKTVMARLGDRLDAVATFNEPWCAVWLSHLYGIHAPGERNMEAALAA
MHHINLAHGFGVEASRHVAPKVPVGLVLNAHSVIPASNSDADMKAAERAF
QFHNGAFFDPVFKGEYPAEMIEALGSRMPVVEAEDLSIISQKLDWWGLNY
YTPMRVADDATEGAEFPATKQAPAVSDVKTDIGWEVYAPALHSLVETLYE
RYELPDCYITENGACYNMGVENGEVDDQPRLDYYAEHLGIVADLVKDGYP
MRGYFAWSLMDNFEWAEGYRMRFGLVHVDYETQVRTLKNSGKWYSALASG
FPK
3D structure
PDB6rjm Agrobacteria reprogram virulence gene expression by controlled release of host-conjugated signals.
ChainA
Resolution2.112 Å
3D
structure
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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 GLC A Q33 H134 E179 Y307 E367 W413 E420 W421 F429 Q27 H128 E173 Y301 E361 W407 E414 W415 F423
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
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6rjm, PDBe:6rjm, PDBj:6rjm
PDBsum6rjm
PubMed31604827
UniProtA0A2I4PGZ0

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