Structure of PDB 1sff Chain C Binding Site BS02

Receptor Information
>1sff Chain C (length=425) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIA
VLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDF
AKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGK
VNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIA
AIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTL
FAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGN
PIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGL
GAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILV
PLTIEDAQIRQGLEIISQCFDEAKQ
Ligand information
Ligand IDIK2
InChIInChI=1S/C10H15N2O8P/c1-6-10(15)8(3-12-19-5-9(13)14)7(2-11-6)4-20-21(16,17)18/h2,12,15H,3-5H2,1H3,(H,13,14)(H2,16,17,18)
InChIKeyQYKRUCBLHROXCK-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNOCC(O)=O)c1O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1CNOCC(=O)O)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNOCC(=O)O)O
FormulaC10 H15 N2 O8 P
Name4'-DEOXY-4'-ACETYLYAMINO-PYRIDOXAL-5'-PHOSPHATE
ChEMBL
DrugBankDB02783
ZINCZINC000002047479
PDB chain1sff Chain C Residue 450 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1sff Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G111 S112 Y138 H139 R141 E206 D239 V241 Q242 K268
Binding residue
(residue number reindexed from 1)		G110 S111 Y137 H138 R140 E205 D238 V240 Q241 K267
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V19 Y138 E206 D239 Q242 K268 T297 R398
Catalytic site (residue number reindexed from 1) V18 Y137 E205 D238 Q241 K267 T296 R397
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate transaminase.
2.6.1.48: 5-aminovalerate transaminase.
Gene Ontology
Molecular Function
GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042803 protein homodimerization activity
GO:0047589 5-aminovalerate transaminase activity
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process
GO:0009450 gamma-aminobutyric acid catabolic process
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1sff, PDBe:1sff, PDBj:1sff
PDBsum1sff
PubMed15323550
UniProtP22256|GABT_ECOLI 4-aminobutyrate aminotransferase GabT (Gene Name=gabT)

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