Structure of PDB 5a2x Chain B

Receptor sequence
>5a2xB (length=467) Species: 9031 (Gallus gallus) [Search protein sequence]
RKKTFTEVQTERLEQADRSVLIKCPSKLNEKKLLQYLSSHGKIDNYFFFE
NRGIHALIEFSEKSSVASLQAVTGIPKHVVPYKSRLFTFTLKNPGSQAEE
RPVKISPQSHIPVNELIPKLCHADSISSQMYILLNEYQLTEENIKLRYLA
CSLVRDFARAYFPDSTVKPFGSSVNTFGKLGCDVDMFLDFHDMKKGPFEM
EYQMKRLPSERLATQKILSIIGDCLDNFGPGYSSVQKILNARCPLVKFSH
QPTGFQCDLSVSNSIAIRCSELLYIYGCLDPRVRALVFSLRCWARVHGLT
NSVPGTWITNFSLTMMIMFFLQKRSPPIIPTLDQLKELADEKDKHVIGGY
DCSFVSDLSKIKPTKNTETLDELLCDFFQYFGNFDFRKNSLNLRKGKEVN
KPESSPLYIWNPFEQDLNISKNVNQPQLEKFVAMARESAWILQKEDKTQQ
MINKEPWGLAAVLIPFG
3D structure
PDB5a2x Structure of Mitochondrial Poly(A) RNA Polymerase Reveals the Structural Basis for Dimerization, ATP Selectivity and the Spax4 Disease Phenotype.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G283 G290 K298 I408 S465
Catalytic site (residue number reindexed from 1) G222 G229 K237 I347 S404
Enzyme Commision number ?
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 CTP B F224 S226 D239 C330 F372 F170 S172 D185 C269 F311
BS02 MG B D237 D239 D183 D185
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0002134 UTP binding
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:1990817 poly(A) RNA polymerase activity
Biological Process
GO:0000965 mitochondrial RNA 3'-end processing
GO:0016070 RNA metabolic process
GO:0071044 histone mRNA catabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
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:5a2x, PDBe:5a2x, PDBj:5a2x
PDBsum5a2x
PubMed26319014
UniProtF1NBW0

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