Structure of PDB 2zc0 Chain B Binding Site BS01

Receptor Information
>2zc0 Chain B (length=405) Species: 2265 (Thermococcus litoralis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDYTKYLAGRANWIKGSALADVMKKASELQKKGVKLISLAAGDPDPELIP
RAVLGEIAKEVLEKEPKSVMYTPANGIPELREELAAFLKKYDHLEVSPEN
IVITIGGTGALDLLGRVLIDPGDVVITENPSYINTLLAFEQLGAKIEGVP
VDNDGMRVDLLEEKIKELKAKGQKVKLIYTIPTGQNPMGVTMSMERRKAL
LEIASKYDLLIIEDTAYNFMRYEGGDIVPLKALDNEGRVIVAGTLSKVLG
TGFRIGWIIAEGEILKKVLMQKQPIDFCAPAISQYIALEYLKRGYFEKYH
LEGALLGYKEKRDIMLKALENHLPNAEFTKPIAGMFVMFFLPEGADGISF
ANELMEREGVVVVPGKPFYTDESGKNAIRLNFSRPSKEEIPIGIKKLAKL
YKEKF
Ligand information
Ligand IDPMP
InChIInChI=1S/C8H13N2O5P/c1-5-8(11)7(2-9)6(3-10-5)4-15-16(12,13)14/h3,11H,2,4,9H2,1H3,(H2,12,13,14)
InChIKeyZMJGSOSNSPKHNH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1CN)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN)c1O
FormulaC8 H13 N2 O5 P
Name4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE;
PYRIDOXAMINE-5'-PHOSPHATE
ChEMBLCHEMBL1235353
DrugBankDB02142
ZINCZINC000001532708
PDB chain2zc0 Chain B Residue 409 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2zc0 Structure of an archaeal alanine:glyoxylate aminotransferase
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G106 G107 T108 Y132 N186 D214 A216 Y217 T244 S246 K247 R254
Binding residue
(residue number reindexed from 1)		G106 G107 T108 Y132 N186 D214 A216 Y217 T244 S246 K247 R254
Annotation score1
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.
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

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

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