Structure of PDB 2fhj Chain A

Receptor sequence
>2fhjA (length=296) Species: 2320 (Methanopyrus kandleri) [Search protein sequence]
MEINGVEIEDTFAEAFEAKMARVLITAASHKWAMIAVKEATGFGTSVIMC
PAEAGIDCGYVPPEETPDGRPGVTIMIGHNDEDELKEQLLDRIGQCVMTA
PTASAFDAMPEAEKEDEDRVGYKLSFFGDGYQEEDELDGRKVWKIPVVEG
EFIVEDSFGITTGVAGGNFYIMAESQPAGLQAAEAAVDAIKGVEGAYAPF
PGGIVASASKVGSKQYDFLPASTNDAYCPTVEDNELPEGVKCVYEIVING
LNEEAVKEAMRVGIEAACQQPGVVKISAGNFGGKLGQYEIHLHDLF
3D structure
PDB2fhj The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.101: formylmethanofuran--tetrahydromethanopterin N-formyltransferase.
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 MFN A Q95 M98 Y122 K123 F126 F127 Q95 M98 Y122 K123 F126 F127
BS02 MFN A S46 I48 M49 F200 S209 L219 P220 S46 I48 M49 F200 S209 L219 P220
BS03 H4Z A F16 G166 S209 K210 V211 E245 F281 F16 G166 S209 K210 V211 E245 F281
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0030270 formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0015948 methanogenesis
GO:0019386 methanogenesis, from carbon dioxide
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:2fhj, PDBe:2fhj, PDBj:2fhj
PDBsum2fhj
PubMed16466742
UniProtQ49610|FTR_METKA Formylmethanofuran--tetrahydromethanopterin formyltransferase (Gene Name=ftr)

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