Structure of PDB 6jc8 Chain A

Receptor sequence
>6jc8A (length=512) Species: 1074250 (Actinoalloteichus sp. WH1-2216-6) [Search protein sequence]
GEPVYADAVLNGWLTSMGLGVEYVRAEGNTVYYLDDEGREVPVLDHACGF
GSLIFGHNHPEIIAHAKAALDAGTVVHAQLSRQPRANQISRILNDIMRRE
TGRDDRYNAIFANSGAEANEICMKHAELERQERITALFAEIDAELDTARE
ALTTGTATLDTASLPLVDVDGVIADIHRHNDERRAERPLFLTLDGSFHGK
LVGSIQLTQNEPWRTPFTALSSPARFLPADEPELIGKIVEDERRSVLTLS
LDKDTVRVVERDFPVVAAIFVEPVRGGSGMKTVTPELAEELHRLRDTLGC
PLVVDEVQTGIGRTGAFFGSALLGIRGDYYTLAKAIGGGIVKNSVALIRQ
DRFLPAMEVIHSSTFAKDGLSASIALKVLEMVEADGGRVYQRVRERGQRL
EAMLESVRADHSDVVSAVWGTGLMLALELRDQSNATSQAIREKAAHGFLG
YVLAGFLLREHHIRVLPAGPRSGFLRFSPSLYITDEEIDRTETALRSLFT
ALRDQDGDRLVL
3D structure
PDB6jc8 Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V26 F207 E282 D315 Q318 K344 R486
Catalytic site (residue number reindexed from 1) V21 F197 E272 D305 Q308 K334 R476
Enzyme Commision number ?
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 PL6 A F55 G120 A121 F207 H208 D315 V317 Q318 K344 F50 G115 A116 F197 H198 D305 V307 Q308 K334
BS02 PL6 A S372 T374 S362 T364
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding

View graph for
Molecular Function
External links
PDB RCSB:6jc8, PDBe:6jc8, PDBj:6jc8
PDBsum6jc8
PubMed32814814
UniProtH8Y6N2

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