Structure of PDB 2frv Chain S

Receptor sequence

>2frvS (length=261) Species: 879 (Megalodesulfovibrio gigas)

KKRPSVVYLHNAECTGCSESVLRTVDPYVDELILDVISMDYHETLMAGAG
HAVEEALHEAIKGDFVCVIEGGIPMGDGGYWGKVGGRNMYDICAEVAPKA
KAVIAIGTCATYGGVQAAKPNPTGTVGVNEALGKLGVKAINIAGCPPNPM
NFVGTVVHLLTKGMPELDKQGRPVMFFGETVHDNCPRLKHFEAGEFATSF
GSPEAKKGYCLYELGCKGPDTYNNCPKQLFNQVNWPVQAGHPCIACSEPN
FWDLYSPFYSA

3D structure

• PDB: 2frv Crystal Structure of the Nickel-Iron Hydrogenase from Desulfovibrio Gigas
• Chain: S
• Resolution: 2.54 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C148 C213 C219 C228
• Catalytic site (residue number reindexed from 1): C145 C210 C216 C225
• 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	S	H185 C188 R190 L191 C213 L214 Y215 C219	H182 C185 R187 L188 C210 L211 Y212 C216
BS02	F3S	S	C228 F233 W238 P239 C246 I247 C249	C225 F230 W235 P236 C243 I244 C246
BS03	SF4	S	E16 C17 G19 C20 G110 C112 C148 P149	E13 C14 G16 C17 G107 C109 C145 P146

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

External links

• PDB: RCSB:2frv, PDBe:2frv, PDBj:2frv
• PDBsum: 2frv
• UniProt: P12943|PHNS_MEGGA Periplasmic [NiFe] hydrogenase small subunit (Gene Name=hydA)