Structure of PDB 2zc0 Chain B

Receptor sequence
>2zc0B (length=405) Species: 2265 (Thermococcus litoralis) [Search protein sequence]
MDYTKYLAGRANWIKGSALADVMKKASELQKKGVKLISLAAGDPDPELIP
RAVLGEIAKEVLEKEPKSVMYTPANGIPELREELAAFLKKYDHLEVSPEN
IVITIGGTGALDLLGRVLIDPGDVVITENPSYINTLLAFEQLGAKIEGVP
VDNDGMRVDLLEEKIKELKAKGQKVKLIYTIPTGQNPMGVTMSMERRKAL
LEIASKYDLLIIEDTAYNFMRYEGGDIVPLKALDNEGRVIVAGTLSKVLG
TGFRIGWIIAEGEILKKVLMQKQPIDFCAPAISQYIALEYLKRGYFEKYH
LEGALLGYKEKRDIMLKALENHLPNAEFTKPIAGMFVMFFLPEGADGISF
ANELMEREGVVVVPGKPFYTDESGKNAIRLNFSRPSKEEIPIGIKKLAKL
YKEKF
3D structure
PDB2zc0 Structure of an archaeal alanine:glyoxylate aminotransferase
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y132 D214 A216 S246
Catalytic site (residue number reindexed from 1) Y132 D214 A216 S246
Enzyme Commision number 2.6.1.44: alanine--glyoxylate 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 PMP B G106 G107 T108 Y132 N186 D214 A216 Y217 T244 S246 K247 R254 G106 G107 T108 Y132 N186 D214 A216 Y217 T244 S246 K247 R254
Gene Ontology
Molecular Function
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process
GO:1901605 alpha-amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2zc0, PDBe:2zc0, PDBj:2zc0
PDBsum2zc0
PubMed18560158
UniProtQ9C4M4

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