Structure of PDB 1ivr Chain A Binding Site BS01

Receptor Information
>1ivr Chain A (length=401) Species: 9031 (Gallus gallus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNC
VRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTV
QGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAY
RYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKEL
ASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAK
NMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASL
ILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIG
MFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT
K
Ligand information
Ligand IDCBA
InChIInChI=1S/C12H17N2O11P/c1-5-8(15)7(6(2-13-5)4-25-26(22,23)24)3-14-12(21,11(19)20)9(16)10(17)18/h2,9,14-16,21H,3-4H2,1H3,(H,17,18)(H,19,20)(H2,22,23,24)/t9-,12+/m0/s1
InChIKeySMJZVFGOJYUMBO-JOYOIKCWSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C](O)([CH](O)C(O)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@]([C@H](C(=O)O)O)(C(=O)O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C@@](O)([C@@H](O)C(O)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C(C(=O)O)O)(C(=O)O)O)O
ACDLabs 10.04O=C(O)C(O)C(O)(C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
FormulaC12 H17 N2 O11 P
NameN-PYRIDOXYL-2,3-DIHYDROXYASPARTIC ACID-5-MONOPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000015604329
PDB chain1ivr Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1ivr Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		I15 V35 G36 S104 G105 T106 W133 N186 D214 A216 Y217 S247 K250 R258 R378
Binding residue
(residue number reindexed from 1)		I15 V35 G36 S104 G105 T106 W133 N186 D214 A216 Y217 S247 K250 R258 R378
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W133 D214 A216 K250
Catalytic site (residue number reindexed from 1) W133 D214 A216 K250
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0006520 amino acid metabolic process
GO:0006531 aspartate metabolic process
GO:0006533 aspartate catabolic process
GO:0006536 glutamate metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ivr, PDBe:1ivr, PDBj:1ivr
PDBsum1ivr
PubMed8952476
UniProtP00508|AATM_CHICK Aspartate aminotransferase, mitochondrial (Gene Name=GOT2)

[Back to BioLiP]