5Y4N

Crystal structure of aerobically purified and anaerobically crystallized D. vulgaris Miyazaki F [NiFe]-hydrogenase

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	AC1
Number of Residues	7
Details	binding site for residue SF4 S 1001

Chain	Residue
L	ARG79
S	CYS17
S	CYS20
S	THR113
S	CYS114
S	CYS150
S	PRO151

---

site_id	AC2
Number of Residues	6
Details	binding site for residue SF4 S 1002

Chain	Residue
S	LEU194
S	CYS216
S	LEU217
S	CYS222
S	HIS188
S	CYS191

---

site_id	AC3
Number of Residues	8
Details	binding site for residue F3S S 1003

Chain	Residue
L	GLN237
S	ASN229
S	CYS231
S	PHE236
S	TRP241
S	CYS249
S	ILE250
S	CYS252

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MPD S 1004

Chain	Residue
L	MET379
S	LEU194
S	ASP198
S	HOH1164
S	HOH1295

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MRD S 1005

Chain	Residue
S	ALA211
S	ARG212
S	GLY214
S	ASP244
S	HOH1148
S	HOH1373

---

site_id	AC6
Number of Residues	6
Details	binding site for residue TRS S 1006

Chain	Residue
S	PHE117
S	ASN134
S	ASN146
S	LEU176
S	HOH1168
S	HOH1256

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MG L 601

Chain	Residue
L	GLU62
L	LEU498
L	HIS552
L	HOH732
L	HOH735
L	HOH744

---

site_id	AC8
Number of Residues	12
Details	binding site for residue NFU L 602

Chain	Residue
L	CYS81
L	CYS84
L	HIS88
L	ALA477
L	PRO478
L	ARG479
L	LEU482
L	VAL500
L	PRO501
L	SER502
L	CSO546
L	CYS549

---

site_id	AC9
Number of Residues	5
Details	binding site for residue MRD L 603

Chain	Residue
L	PRO359
L	LYS360
L	TYR361
S	ALA82
S	TYR86

---

site_id	AD1
Number of Residues	6
Details	binding site for residue MRD L 604

Chain	Residue
L	ARG71
L	GLU348
L	TRP463
L	HOH767
L	HOH1007
L	HOH1100

---

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

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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

Chain	Residue	Details
L	CSO546
L	CYS549
L	HIS552
S	CYS222
S	CYS231
S	CYS249
S	CYS252
L	GLU62
L	CYS81
L	CYS84
L	LEU498

---