Structure of PDB 3tw6 Chain A

Receptor sequence
>3tw6A (length=1007) Species: 347834 (Rhizobium etli CFN 42) [Search protein sequence]
GPISKILVANRSEIAIRVFRAANELGIKTVAIWAEEDKLALHRFKADESY
QVGRGPHLARDLGPIESYLSIDEVIRVAKLSGADAIHPGYGLLSESPEFV
DACNKAGIIFIGPKADTMRQLGNKVAARNLAISVGVPVVPATEPKLVERA
RHVESQILGDTHGNVVHLFERDCSVQRRNQKVVERAPAPYLSEAQRQELA
AYSLKIAGATNYIGAGTVEYLMDADTGKFYFIEVNPRIQVEHTVTEVVTG
IDIVKAQIHILDGAAIGTPQSGVPNQEDIRLNGHALQCRVTTEDPEHNFI
PDYGRITAYRSASGFGIRLDGGTSYSGAIITRYYDPLLVKVTAWAPNPLE
AISRMDRALREFRIRGVATNLTFLEAIIGHPKFRDNSYTTRFIDTTPELF
QQVKRQDRATKLLTYLADVTVNGHPEAKDRPKPLENAARPVVPYANGNGV
KDGTKQLLDTLGPKKFGEWMRNEKRVLLTDTTMRDGHQSLLATRMRTYDI
ARIAGTYSHALPNLLSLECWGGATFDVSMRFLTEDPWERLALIREGAPNL
LLQMLLRGANGVGYTNYPDNVVKYFVRQAAKGGIDLFRVFDCLNWVENMR
VSMDAIAEENKLCEAAICYTGDILNSARPKYDLKYYTNLAVELEKAGAHI
IAVKDMAGLLKPAAAKVLFKALREATGLPIHFHTHDTSGIAAATVLAAVE
AGVDAVDAAMDALSGNTSQPCLGSIVEALSGSERDPGLDPAWIRRISFYW
EAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHQV
AQAYADANQMFGDIVKVAPSSKVVGDMALMMVSQDLTVADVVSPDREVSF
PESVVSMLKGDLGQPPSGWPEALQKKALKGEKPYTVRPGSLLKEADLDAE
RKVIEKKLEREVSDFEFASYLMYPKVFTDFALASDTYGPVSVLPTPAYFY
GLADGEELFADIEKGKTLVIVNQAVSATDSQGMVTVFFELNGQPRRIKVP
DRAHGAT
3D structure
PDB3tw6 Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli.
ChainA
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) K124 H216 R242 T281 E283 E297 N299 R301 E305 R353 D549 D655 K718 H747 H749 A882
Catalytic site (residue number reindexed from 1) K124 H152 R178 T217 E219 E233 N235 R237 E241 R289 D485 D591 K654 H683 H685 A818
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 ADP A L210 V211 H216 Q240 N243 L285 L146 V147 H152 Q176 N179 L221
BS02 ZN A D549 K718 H747 H749 D485 K654 H683 H685
BS03 MG A E283 E297 E219 E233
BS04 MG A M534 R535 E537 D768 M470 R471 E473 D704
BS05 COA A R429 R469 Q470 D471 R472 T1031 L1032 R365 R405 Q406 D407 R408 T967 L968
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004736 pyruvate carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006090 pyruvate metabolic process
GO:0006094 gluconeogenesis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tw6, PDBe:3tw6, PDBj:3tw6
PDBsum3tw6
PubMed21958016
UniProtQ2K340

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