Structure of PDB 4m6v Chain B

Receptor sequence
>4m6vB (length=593) Species: 347834 (Rhizobium etli CFN 42) [Search protein sequence]
DRATKLLTYLADVTVNGHPEAKDRPKPLENARPVVPYAGVKDGTKQLLDT
LGPKKFGEWMRNEKRVLLTDTTMRDGHQSLLATRMRTYDIARIAGTYSHA
LPNLLSLECWGGATFDVSMRFLTEDPWERLALIREGAPNLLLQMLLRGAN
GVGYTNYPDNVVKYFVRQAAKGGIDLFRVFDCLNWVENMRVSMDAIAEEN
KLCEAAICYTGDILNSARPKYDLKYYTNLAVELEKAGAHIIAVKDMAGLL
KPAAAKVLFKALREATGLPIHFHTHDTSGIAAATVLAAVEAGVDAVDAAM
DALSGNTSQPCLGSIVEALSGSERDPGLDPAWIRRISFYWEAVRNQYAAF
ESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHQVAQAYADANQM
FGDIVKVTPSSKVVGDMALMMVSQDLTVADVVSPDREVSFPESVVSMLKG
DLGQPPSGWPEALQKKALKGEKPYTVRPGSLLKEADLDAERKVIEKKLER
EVSDFEFASYLMYPKVFTDFALASDTYGPVSVLPTPAYFYGLADGEELFA
DIEKGKTLVIVNQAVSATDSQGMVTVFFELNGQPRRIKVPDRA
3D structure
PDB4m6v The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D549 D655 K718 H747 H749 T882
Catalytic site (residue number reindexed from 1) D75 D181 K244 H273 H275 T408
Enzyme Commision number 6.4.1.1: pyruvate carboxylase.
Interaction with ligand
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

View graph for
Biological Process
External links
PDB RCSB:4m6v, PDBe:4m6v, PDBj:4m6v
PDBsum4m6v
PubMed25157442
UniProtQ2K340

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