Structure of PDB 4ce5 Chain B

Receptor sequence

>4ce5B (length=325) Species: 33178 (Aspergillus terreus) [Search protein sequence]

MASMDKVFAGYAARQAILESTETTNPFAKGIAWVEGELVPLAEARIPLLD
QGFMHSDLTYDVPSVWDGRFFRLDDHITRLEASCTKLRLRLPLPRDQVKQ
ILVEMVAKSGIRDAFVELIVTRGLKGVRGTRPEDIVNNLYMFVQPYVWVM
EPDMQRVGGSAVVARTVRRVPPGAIDPTVKNLQWGDLVRGMFEAADRGAT
YPFLTDGDAHLTEGSGFNIVLVKDGVLYTPDRGVLQGVTRKSVINAAEAF
GIEVRVEFVPVELAYRCDEIFMCTTAGGIMPITTLDGMPVNGGQIGPITK
KIWDGYWAMHYDAAYSFEIDYNERN

3D structure

PDB

4ce5 Crystal Structure of an (R)-Selective Omega-Transaminase from Aspergillus Terreus

Chain

Resolution

1.63 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)
BS01	PLP	B	R79 K180 E213 G216 F217 L235 G237 V238 T239 T275	R79 K180 E213 G216 F217 L235 G237 V238 T239 T275
BS02	PDG	B	V62 R79 K180 W184 E213 G216 F217 N218 L235 G237 V238 T239 T274 T275 A276	V62 R79 K180 W184 E213 G216 F217 N218 L235 G237 V238 T239 T274 T275 A276
BS03	CA	B	D67 R69	D67 R69

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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:4ce5, PDBe:4ce5, PDBj:4ce5
PDBsum	4ce5
PubMed	24498081
UniProt	Q0C8G1

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