4TTT

Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form - oxidized state 3

Functional Information from GO Data

Chain	GOid	namespace	contents
L	0005515	molecular_function	protein binding
L	0005886	cellular_component	plasma membrane
L	0008901	molecular_function	ferredoxin hydrogenase activity
L	0016020	cellular_component	membrane
L	0016151	molecular_function	nickel cation binding
L	0016491	molecular_function	oxidoreductase activity
L	0033748	molecular_function	hydrogenase (acceptor) activity
L	0046872	molecular_function	metal ion binding
S	0005515	molecular_function	protein binding
S	0005886	cellular_component	plasma membrane
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	0033748	molecular_function	hydrogenase (acceptor) activity
S	0044569	cellular_component	[Ni-Fe] hydrogenase complex
S	0046872	molecular_function	metal ion binding
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	AC1
Number of Residues	13
Details	binding site for residue NFV L 701

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	ARG53-CYS78

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

Chain	Residue	Details
L	PHE594-HIS603

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	11
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P21853