Structure of PDB 1h0c Chain A Binding Site BS01

Receptor Information
>1h0c Chain A (length=385) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDM
YQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG
ANGIWGQRAVDIGERIGVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTH
GESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYS
GSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDD
QPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQAL
GLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPST
GKVLRIGLLGCNATRENVDRVTEALRAALQHCPKK
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1h0c Chain A Residue 1391 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1h0c Crystal Structure of Alanine:Glyoxylate Aminotransferase and the Relationship between Genotype and Enzymatic Phenotype in Primary Hyperoxaluria Type 1.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		S81 G82 H83 W108 S158 D183 V185 K209 K390
Binding residue
(residue number reindexed from 1)		S78 G79 H80 W105 S153 D178 V180 K204 K385
Annotation score1
Enzymatic activity
Enzyme Commision number 2.6.1.44: alanine--glyoxylate transaminase.
2.6.1.51: serine--pyruvate transaminase.
Gene Ontology
Molecular Function
GO:0004760 L-serine-pyruvate transaminase activity
GO:0005515 protein binding
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0016597 amino acid binding
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006563 L-serine metabolic process
GO:0007219 Notch signaling pathway
GO:0009436 glyoxylate catabolic process
GO:0019265 glycine biosynthetic process, by transamination of glyoxylate
GO:0019448 L-cysteine catabolic process
GO:0042853 L-alanine catabolic process
GO:0046487 glyoxylate metabolic process
GO:0046724 oxalic acid secretion
Cellular Component
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h0c, PDBe:1h0c, PDBj:1h0c
PDBsum1h0c
PubMed12899834
UniProtP21549|AGT1_HUMAN Alanine--glyoxylate aminotransferase (Gene Name=AGXT)

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