Structure of PDB 1h0c Chain A

Receptor sequence
>1h0cA (length=385) Species: 9606 (Homo sapiens) [Search protein sequence]
HKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDM
YQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG
ANGIWGQRAVDIGERIGVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTH
GESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYS
GSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDD
QPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQAL
GLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPST
GKVLRIGLLGCNATRENVDRVTEALRAALQHCPKK
3D structure
PDB1h0c Crystal Structure of Alanine:Glyoxylate Aminotransferase and the Relationship between Genotype and Enzymatic Phenotype in Primary Hyperoxaluria Type 1.
ChainA
Resolution2.5 Å
3D
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Enzymatic activity
Enzyme Commision number 2.6.1.44: alanine--glyoxylate transaminase.
2.6.1.51: serine--pyruvate 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 PLP A S81 G82 H83 W108 S158 D183 V185 K209 K390 S78 G79 H80 W105 S153 D178 V180 K204 K385
BS02 AOA A P28 G29 L351 R360 P25 G26 L346 R355
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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