Structure of PDB 2yob Chain A

Receptor sequence
>2yobA (length=385) Species: 9606 (Homo sapiens) [Search protein sequence]
HKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDM
YQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG
ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFL
THGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDIL
YSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGC
DDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQ
ALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVMDHFDIEIMGGLGP
STGKVLRIGLLGCNATRENVDRVTEALRAALVAQA
3D structure
PDB2yob The Role of Protein Denaturation Energetics and Molecular Chaperones in the Aggregation and Mistargeting of Mutants Causing Primary Hyperoxaluria Type I
ChainA
Resolution1.9 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 A186 Q208 K209 S78 G79 H80 W105 S155 D180 V182 A183 Q205 K206
BS02 PLP A Y260 T263 Y257 T260
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:2yob, PDBe:2yob, PDBj:2yob
PDBsum2yob
PubMed24205397
UniProtP21549|AGT1_HUMAN Alanine--glyoxylate aminotransferase (Gene Name=AGXT)

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