Structure of PDB 3bg9 Chain C

Receptor sequence

>3bg9C (length=601) Species: 9606 (Homo sapiens)

QNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAGFRD
ILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPY
VAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL
RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAA
GSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDM
AGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADV
VDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARG
LYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKA
YVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRS
VVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKE
LVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPK
IAEEFEVELERGKTLHIKALAVSDLNRAGQRQVAFELNGQLRSILVKDTQ
A

3D structure

• PDB: 3bg9 Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
• Chain: C
• Resolution: 3.0 Å

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	C	D572 K741 H771 H773	D79 K248 H278 H280

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

External links

• PDB: RCSB:3bg9, PDBe:3bg9, PDBj:3bg9
• PDBsum: 3bg9
• PubMed: 18297087
• UniProt: P11498|PYC_HUMAN Pyruvate carboxylase, mitochondrial (Gene Name=PC)