Structure of PDB 3bg3 Chain D

Receptor sequence
>3bg3D (length=680) Species: 9606 (Homo sapiens) [Search protein sequence]
QNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAGFRD
ILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPY
VAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL
RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAA
GSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDM
AGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADV
VDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARG
LYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKA
YVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRS
VVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKE
LVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPK
IAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQ
AMKEKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETV
VTSPMEGTVRKVHVTKDMTLEGDDLILEIE
3D structure
PDB3bg3 Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
ChainD
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D572 D678 K741 H771 H773 T908
Catalytic site (residue number reindexed from 1) D79 D185 K248 H278 H280 T415
Enzyme Commision number 6.4.1.1: pyruvate carboxylase.
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 MN D D572 K741 H771 H773 D79 K248 H278 H280
BS02 PYR D R571 Q575 L642 R644 K741 R78 Q82 L149 R151 K248
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004736 pyruvate carboxylase activity
GO:0005524 ATP binding
Biological Process
GO:0006090 pyruvate metabolic process
GO:0006094 gluconeogenesis

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Molecular Function
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Biological Process
External links
PDB RCSB:3bg3, PDBe:3bg3, PDBj:3bg3
PDBsum3bg3
PubMed18297087
UniProtP11498|PYC_HUMAN Pyruvate carboxylase, mitochondrial (Gene Name=PC)

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