Structure of PDB 3myr Chain G

Receptor sequence
>3myrG (length=268) Species: 1049 (Allochromatium vinosum) [Search protein sequence]
ARRPSVIWLSFQECTGCTESLTRAHAPTLEDLILDFISLDYHHTLQAASG
EAAEAARLQAMDENRGQYLVIVDGSIPGPDANPGFSTVAGHSNYSILMET
VEHAAAVIAVGTCAAFGGLPQARPNPTGAMSVMDLVRDKPVINVPGCPPI
PMVITGVIAHYLVFGRLPELDGYGRPLAFYGQSIHDRCYRRPFYDKGLFA
ESFDDEGAKQGWCLYRLGCKGPTTYNACATMKWNDGTSWPVEAGHPCLGC
SEPQFWDAGGFYEPVSVP
3D structure
PDB3myr The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A state).
ChainG
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C16 C19 C115 C149 H187 C190 C215 C221 C230 P242 C249 C252
Catalytic site (residue number reindexed from 1) C14 C17 C113 C147 H185 C188 C213 C219 C228 P240 C247 C250
Enzyme Commision number 1.12.99.6: hydrogenase (acceptor).
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 SF4 G E15 C16 G18 C19 G113 C115 C149 P150 E13 C14 G16 C17 G111 C113 C147 P148
BS02 SF4 G H187 C190 R192 R193 C215 L216 Y217 C221 H185 C188 R190 R191 C213 L214 Y215 C219
BS03 F3S G N228 C230 W235 W241 P242 C249 L250 C252 N226 C228 W233 W239 P240 C247 L248 C250
Gene Ontology
Molecular Function
GO:0008901 ferredoxin hydrogenase activity
GO:0051536 iron-sulfur cluster binding
Cellular Component
GO:0009375 ferredoxin hydrogenase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:3myr, PDBe:3myr, PDBj:3myr
PDBsum3myr
PubMed20673834
UniProtD3RV29

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