Structure of PDB 6gio Chain B

Receptor sequence
>6gioB (length=435) Species: 529 (Brucella anthropi) [Search protein sequence]
TPLSLRERDARVIAEIGRLRFSPLSLIGGKGNRLIEEGGRSILDLSGSAG
PAALGYGHPAIVEAVEKSVRDMAGASLLLYPNEAAVSLAEDLLRITPGNG
ERRVWFGHSGSDANDCAVRVLTAATKRSRIISFIGSYHGNLTGSMGISGH
TAMTHTLPRPGVLLLPYPDPFRPRFSAEAVLELLDYHFATSCPPEQVAAV
FIEPILSDGGLVVPPPAFLEALQDRCRKHGILVVVDEVKVGLGRTGLMHC
FQHEGLEPDMVVFGKGLGGGLPLSAVVGPQWVMDHAPAFVLQTTAGNPVA
TAAGRAVLNTIERQGLAQRSERVGGIFADRLRRLSDKHSIIGDVRGRGLA
IGVDLVSDRGSREPAPVTTTAKIIYRGYQLGAAFTYVGLNANVLEFMPPL
TLTEPEIDEAADIVDQAIGDVLDGKVADSDVAHFM
3D structure
PDB6gio An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity.
ChainB
Resolution1.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G19 Y139 D238 K267
Catalytic site (residue number reindexed from 1) G17 Y137 D236 K265
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 PLP B S111 G112 S113 Y139 H140 D238 V240 K241 K267 S109 G110 S111 Y137 H138 D236 V238 K239 K265
Gene Ontology
Molecular Function
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0019481 L-alanine catabolic process, by transamination

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Molecular Function
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Biological Process
External links
PDB RCSB:6gio, PDBe:6gio, PDBj:6gio
PDBsum6gio
PubMed29897155
UniProtQ06K28

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