5XVC

[NiFe]-hydrogenase (Hyb-type) from Citrobacter sp. S-77 in a ferricyanide-oxidized condition

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0046872	molecular_function	metal ion binding
M	0005886	cellular_component	plasma membrane
M	0008901	molecular_function	ferredoxin hydrogenase activity
M	0016020	cellular_component	membrane
M	0016151	molecular_function	nickel cation binding
M	0016491	molecular_function	oxidoreductase activity
M	0046872	molecular_function	metal ion binding
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
T	0008901	molecular_function	ferredoxin hydrogenase activity
T	0009055	molecular_function	electron transfer activity
T	0009061	biological_process	anaerobic respiration
T	0009375	cellular_component	ferredoxin hydrogenase complex
T	0016020	cellular_component	membrane
T	0016491	molecular_function	oxidoreductase activity
T	0033748	molecular_function	hydrogenase (acceptor) activity
T	0044569	cellular_component	[Ni-Fe] hydrogenase complex
T	0046872	molecular_function	metal ion binding
T	0051536	molecular_function	iron-sulfur cluster binding
T	0051538	molecular_function	3 iron, 4 sulfur cluster binding
T	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 601

Chain	Residue
L	GLU42
L	ALA498
L	HIS552
L	HOH708
L	HOH738
L	HOH764

---

site_id	AC2
Number of Residues	13
Details	binding site for residue NFV L 602

Chain	Residue
L	HIS68
L	ALA477
L	PRO478
L	ARG479
L	LEU482
L	VAL500
L	PRO501
L	SER502
L	CSO546
L	CYS549
L	CYS61
L	CYS64
L	THR67

---

site_id	AC3
Number of Residues	8
Details	binding site for residue PEG L 603

Chain	Residue
L	GLN178
L	TYR269
L	PRO270
L	GLU271
L	TRP272
L	ARG275
L	PRO526
L	HOH847

---

site_id	AC4
Number of Residues	6
Details	binding site for residue SF4 S 500

Chain	Residue
S	HIS192
S	CYS195
S	ARG198
S	CYS220
S	LEU221
S	CYS226

---

site_id	AC5
Number of Residues	9
Details	binding site for residue F3S S 501

Chain	Residue
L	LYS211
L	GLN216
S	CYS235
S	PHE240
S	CYS255
S	TYR256
S	GLY257
S	CYS258
S	ASN259

---

site_id	AC6
Number of Residues	12
Details	binding site for residue 8JU S 502

Chain	Residue
S	CYS22
S	THR23
S	GLY24
S	CYS25
S	ASP81
S	GLY118
S	SER119
S	CYS120
S	GLY153
S	CYS154
S	PRO155
S	HOH619

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MG M 700

Chain	Residue
M	GLU42
M	ALA498
M	HIS552
M	HOH821
M	HOH875
M	HOH876

---

site_id	AC8
Number of Residues	13
Details	binding site for residue NFV M 701

Chain	Residue
M	CYS61
M	CYS64
M	THR67
M	HIS68
M	ALA477
M	PRO478
M	ARG479
M	LEU482
M	VAL500
M	PRO501
M	SER502
M	CSO546
M	CYS549

---

site_id	AC9
Number of Residues	7
Details	binding site for residue SF4 T 500

Chain	Residue
T	HIS192
T	CYS195
T	ARG197
T	ARG198
T	CYS220
T	LEU221
T	CYS226

---

site_id	AD1
Number of Residues	9
Details	binding site for residue F3S T 501

Chain	Residue
M	GLN216
T	ILE191
T	CYS235
T	PHE240
T	CYS255
T	TYR256
T	GLY257
T	CYS258
T	ASN259

---

site_id	AD2
Number of Residues	12
Details	binding site for residue 8JU T 502

Chain	Residue
T	PRO155
T	HOH610
T	CYS22
T	THR23
T	GLY24
T	CYS25
T	ASP81
T	GLY82
T	SER119
T	CYS120
T	GLY153
T	CYS154

---

site_id	AD3
Number of Residues	14
Details	binding site for Di-peptide PRO M 545 and CSO M 546

Chain	Residue
M	ILE13
M	GLU14
M	CYS61
M	SER502
M	TYR518
M	ILE540
M	PHE543
M	ASP544
M	MET547
M	SER548
M	CYS549
M	ALA550
M	NFV701
M	HOH869

---

site_id	AD4
Number of Residues	14
Details	binding site for Di-peptide CSO M 546 and MET M 547

Chain	Residue
M	GLU14
M	HIS16
M	LEU17
M	GLY35
M	CYS61
M	SER502
M	ASP544
M	PRO545
M	SER548
M	CYS549
M	ALA550
M	VAL551
M	NFV701
M	HOH814

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	ARG39-CYS64

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

Chain	Residue	Details
L	PHE543-HIS552

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