Structure of PDB 3daf Chain A

Receptor sequence
>3dafA (length=344) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MKIAILGAGCYRTHAAAGITNFMRACEVAKEVGKPEIALTHSSITYGAEL
LHLVPDVKEVIVSDPCFAEEPGLVVIDEFDPKEVMEAHLSGNPESIMPKI
REVVKAKAKELPKPPKACIHLVHPEDVGLKVTSDDREAVEGADIVITWLP
KGNKQPDIIKKFADAIPEGAIVTHACTIPTTKFAKIFKDLGREDLNITSY
HPGCVPEMKGQVYIAEGYASEEAVNKLYEIGKIARGKAFKMPANLIGPVC
DMCSAVTATVYAGLLAYRDAVTKILGAPADFAQMMADEALTQIHNLMKEK
GIANMEEALDPAALLGTADSMCFGPLAEILPTALKVLEVHKVVE
3D structure
PDB3daf The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.12.98.2: 5,10-methenyltetrahydromethanopterin hydrogenase.
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 CMO A W148 C176 P202 W148 C176 P202
BS02 CMO A W148 C204 V205 W148 C204 V205
BS03 FEG A G7 G9 T13 H14 S63 D64 P65 P114 P115 C118 D135 W148 L149 P150 I158 C176 T177 G7 G9 T13 H14 S63 D64 P65 P114 P115 C118 D135 W148 L149 P150 I158 C176 T177
Gene Ontology
Molecular Function
GO:0004735 pyrroline-5-carboxylate reductase activity
GO:0016491 oxidoreductase activity
GO:0047068 N5,N10-methenyltetrahydromethanopterin hydrogenase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0015948 methanogenesis
GO:0019386 methanogenesis, from carbon dioxide
GO:0055129 L-proline biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3daf, PDBe:3daf, PDBj:3daf
PDBsum3daf
PubMed18653896
UniProtQ58194|HMD_METJA 5,10-methenyltetrahydromethanopterin hydrogenase (Gene Name=hmd)

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