1H2R

THREE-DIMENSIONAL STRUCTURE OF NI-FE HYDROGENASE FROM DESULFIVIBRIO VULGARIS MIYAZAKI F IN THE REDUCED FORM AT 1.4 A RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
L	0008901	molecular_function	ferredoxin hydrogenase activity
L	0016151	molecular_function	nickel cation binding
L	0016491	molecular_function	oxidoreductase activity
L	0042597	cellular_component	periplasmic space
L	0046872	molecular_function	metal ion binding
L	0047806	molecular_function	cytochrome-c3 hydrogenase activity
S	0008901	molecular_function	ferredoxin hydrogenase activity
S	0009055	molecular_function	electron transfer activity
S	0009061	biological_process	anaerobic respiration
S	0009375	cellular_component	ferredoxin hydrogenase complex
S	0016020	cellular_component	membrane
S	0016491	molecular_function	oxidoreductase activity
S	0042597	cellular_component	periplasmic space
S	0044569	cellular_component	[Ni-Fe] hydrogenase complex
S	0046872	molecular_function	metal ion binding
S	0047806	molecular_function	cytochrome-c3 hydrogenase activity
S	0051536	molecular_function	iron-sulfur cluster binding
S	0051538	molecular_function	3 iron, 4 sulfur cluster binding
S	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NFE L 1004

Functional Information from PROSITE/UniProt

site_id	PS00507
Number of Residues	26
Details	NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilkgrdprdaqhftQRtCGVC

Chain	Residue	Details
L	ARG59-CYS84

site_id	PS00508
Number of Residues	10
Details	NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCIACgv.H

Chain	Residue	Details
L	PHE543-HIS552

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269\|PubMed:10378274, ECO:0000269\|PubMed:9438867, ECO:0007744\|PDB:1H2A, ECO:0007744\|PDB:1H2R