Structure of PDB 1e3d Chain C

Receptor sequence
>1e3dC (length=262) Species: 876 (Desulfovibrio desulfuricans) [Search protein sequence]
SRPSVVYLHAAECTGCSEALLRTYQPFIDTLILDTISLDYHETIMAAAGE
AAEEALQAAVNGPDGFICLVEGAIPTGMDNKYGYIAGHTMYDICKNILPK
AKAVVSIGTCACYGGIQAAKPNPTAAKGINDCYADLGVKAINVPGCPPNP
LNMVGTLVAFLKGQKIELDEVGRPVMFFGQSVHDLCERRKHFDAGEFAPS
FNSEEARKGWCLYDVGCKGPETYNNCPKVLFNETNWPVAAGHPCIGCSEP
NFWDDMTPFYQN
3D structure
PDB1e3d [Nife] Hydrogenase from Desulfovibrio Desulfuricans Atcc 27774: Gene Sequencing, Three-Dimensional Structure Determination and Refinement at 1.8 A and Modelling Studies of its Interaction with the Tetrahaem Cytochrome C3.
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C17 C20 C114 C150 H187 C190 C215 C221 C230 P241 C248 C251
Catalytic site (residue number reindexed from 1) C13 C16 C110 C146 H183 C186 C211 C217 C226 P237 C244 C247
Enzyme Commision number 1.12.2.1: cytochrome-c3 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 F3S C N228 C230 F235 W240 P241 C248 I249 C251 N224 C226 F231 W236 P237 C244 I245 C247
BS02 SF4 C H187 C190 R192 R193 C215 L216 Y217 C221 H183 C186 R188 R189 C211 L212 Y213 C217
BS03 FSX C E16 C17 G19 C20 E75 G112 C114 C150 P151 E12 C13 G15 C16 E71 G108 C110 C146 P147
Gene Ontology
Molecular Function
GO:0008901 ferredoxin hydrogenase activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0047806 cytochrome-c3 hydrogenase activity
GO:0051536 iron-sulfur cluster binding
GO:0051538 3 iron, 4 sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0009061 anaerobic respiration
Cellular Component
GO:0009375 ferredoxin hydrogenase complex
GO:0016020 membrane
GO:0042597 periplasmic space
GO:0044569 [Ni-Fe] hydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e3d, PDBe:1e3d, PDBj:1e3d
PDBsum1e3d
PubMed11191224
UniProtQ9L869

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