Structure of PDB 4urh Chain A

Receptor sequence
>4urhA (length=263) Species: 878 (Solidesulfovibrio fructosivorans) [Search protein sequence]
TAKHRPSVVWLHNAECTGCTEAAIRTIKPYIDALILDTISLDYQETIMAA
AGEAAEAALHQALEGKDGYYLVVEGGLPTIDGGQWGMVAGHPMIETTKKA
AAKAKGIICIGTCSAYGGVQKAKPNPSQAKGVSEALGVKTINIPGCPPNP
INFVGAVVHVLTKGIPDLDENGRPKLFYGELVHDNCPRLPHFEASEFAPS
FDSEEAKKGFCLYELGCKGPVTYNNCPKVLFNQVNWPVQAGHPCLGCSEP
DFWDTMTPFYEQG
3D structure
PDB4urh Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized states.
ChainA
Resolution1.44 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C17 C20 C114 C147 H184 C187 C212 C218 C227 P238 C245 C248
Catalytic site (residue number reindexed from 1) C16 C19 C113 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 SF4 A H184 C187 R189 L190 C212 L213 Y214 C218 P221 H183 C186 R188 L189 C211 L212 Y213 C217 P220
BS02 F3S A N225 C227 F232 W237 P238 C245 L246 C248 N224 C226 F231 W236 P237 C244 L245 C247
BS03 SF4 A E16 C17 G19 C20 G112 C114 C147 P148 E15 C16 G18 C19 G111 C113 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4urh, PDBe:4urh, PDBj:4urh
PDBsum4urh
PubMed25315838
UniProtP18187|PHNS_SOLFR Periplasmic [NiFe] hydrogenase small subunit (Gene Name=hydA)

[Back to BioLiP]