Structure of PDB 4ce5 Chain A

Receptor sequence
>4ce5A (length=325) Species: 33178 (Aspergillus terreus) [Search protein sequence]
MASMDKVFAGYAARQAILESTETTNPFAKGIAWVEGELVPLAEARIPLLD
QGFMHSDLTYDVPSVWDGRFFRLDDHITRLEASCTKLRLRLPLPRDQVKQ
ILVEMVAKSGIRDAFVELIVTRGLKGVRGTRPEDIVNNLYMFVQPYVWVM
EPDMQRVGGSAVVARTVRRVPPGAIDPTVKNLQWGDLVRGMFEAADRGAT
YPFLTDGDAHLTEGSGFNIVLVKDGVLYTPDRGVLQGVTRKSVINAAEAF
GIEVRVEFVPVELAYRCDEIFMCTTAGGIMPITTLDGMPVNGGQIGPITK
KIWDGYWAMHYDAAYSFEIDYNERN
3D structure
PDB4ce5 Crystal Structure of an (R)-Selective Omega-Transaminase from Aspergillus Terreus
ChainA
Resolution1.63 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y60 K180 E213 L235
Catalytic site (residue number reindexed from 1) Y60 K180 E213 L235
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
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 PLP A R79 K180 E213 F217 L235 G237 V238 T239 T275 R79 K180 E213 F217 L235 G237 V238 T239 T275
BS02 PDG A Y60 V62 R79 K180 W184 E213 G216 F217 N218 L235 G237 V238 T239 T274 T275 Y60 V62 R79 K180 W184 E213 G216 F217 N218 L235 G237 V238 T239 T274 T275
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0046872 metal ion binding
Biological Process
GO:0019752 carboxylic acid metabolic process
GO:0046394 carboxylic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4ce5, PDBe:4ce5, PDBj:4ce5
PDBsum4ce5
PubMed24498081
UniProtQ0C8G1

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