Structure of PDB 6jc9 Chain D

Receptor sequence
>6jc9D (length=508) Species: 1074250 (Actinoalloteichus sp. WH1-2216-6) [Search protein sequence]
GEPVYADAVLNGWLTSMGLGVEYVRAEGNTVYYLDDEGREVPVLDHACGF
GSLIFGHNHPEIIAHAKAALDAGTVVHAQLSRQPRANQISRILNDIMRRE
TGRDDRYNAIFANSGAEANEICMKHAELERQERITALFAEIDAELDTARE
ALTTGTATLDTLPLVDVDGVIADIHRHNDERRAERPLFLTLDGSFHGKLV
GSIQLTQNEPWRTPFTALSSPARFLPADEPELIGKIVEDERRSVLTLSLD
TVRVVERDFPVVAAIFVEPVRGGSGMKTVTPELAEELHRLRDTLGCPLVV
DEVQTGIGRTGAFFGSALLGIRGDYYTLAKAIGGGIVKNSVALIRQDRFL
PAMEVIHSSTFAKDGLSASIALKVLEMVEADGGRVYQRVRERGQRLEAML
ESVRADHSDVVSAVWGTGLMLALELRDQSNATSQAIREKAAHGFLGYVLA
GFLLREHHIRVLPAGPRSGFLRFSPSLYITDEEIDRTETALRSLFTALRD
QDGDRLVL
3D structure
PDB6jc9 Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.
ChainD
Resolution2.35 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 F195 E268 D301 Q304 K330 R472
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 GLN D F55 F207 K344 F50 F195 K330
BS02 PLP D S119 G120 A121 F207 E282 D315 V317 Q318 K344 S114 G115 A116 F195 E268 D301 V303 Q304 K330
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:6jc9, PDBe:6jc9, PDBj:6jc9
PDBsum6jc9
PubMed32814814
UniProtH8Y6N2

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