5MDK

Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form (oxidized state - 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	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	6
Details	binding site for residue MG L 701

Chain	Residue
L	GLU56
L	CYS549
L	HIS603
L	HOH814
L	HOH827
L	HOH829

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CL L 702

Chain	Residue
L	GLN548
L	HOH1098
L	LYS60
L	VAL369
L	THR370

---

site_id	AC3
Number of Residues	1
Details	binding site for residue CL L 703

Chain	Residue
L	GLN459

---

site_id	AC4
Number of Residues	13
Details	binding site for residue NFV L 704

Chain	Residue
L	CYS75
L	CYS78
L	CYS81
L	HIS82
L	ALA528
L	PRO529
L	ARG530
L	LEU533
L	VAL551
L	PRO552
L	THR553
L	CYS597
L	CYS600

---

site_id	AC5
Number of Residues	3
Details	binding site for residue CL S 401

Chain	Residue
S	TRP118
S	CYS120
S	GLY256

---

site_id	AC6
Number of Residues	7
Details	binding site for residue SF4 S 402

Chain	Residue
S	HIS187
S	CYS190
S	ARG193
S	CYS215
S	LEU216
S	CYS221
S	ILE243

---

site_id	AC7
Number of Residues	9
Details	binding site for residue F3S S 403

Chain	Residue
L	LYS226
S	THR226
S	ASN228
S	CYS230
S	TRP235
S	PRO242
S	CYS249
S	ILE250
S	CYS252

---

site_id	AC8
Number of Residues	11
Details	binding site for residue F4S S 404

Chain	Residue
S	GLU16
S	CYS17
S	THR18
S	CYS19
S	CYS20
S	GLU76
S	SER114
S	CYS115
S	CYS120
S	GLY148
S	CYS149

---

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P21853","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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