Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6GAL

Structure of fully reduced Hydrogenase (Hyd-1) variant E28Q collected at pH 10

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	0009055	molecular_function	electron transfer activity
L	0009061	biological_process	anaerobic respiration
L	0009267	biological_process	cellular response to starvation
L	0016020	cellular_component	membrane
L	0016151	molecular_function	nickel cation binding
L	0016491	molecular_function	oxidoreductase activity
L	0019645	biological_process	anaerobic electron transport chain
L	0030288	cellular_component	outer membrane-bounded periplasmic space
L	0033748	molecular_function	hydrogenase (acceptor) activity
L	0044569	cellular_component	[Ni-Fe] hydrogenase complex
L	0046872	molecular_function	metal ion binding
L	0098567	cellular_component	periplasmic side of plasma membrane
L	1902421	biological_process	hydrogen metabolic process
M	0005515	molecular_function	protein binding
M	0005886	cellular_component	plasma membrane
M	0008901	molecular_function	ferredoxin hydrogenase activity
M	0009055	molecular_function	electron transfer activity
M	0009061	biological_process	anaerobic respiration
M	0009267	biological_process	cellular response to starvation
M	0016020	cellular_component	membrane
M	0016151	molecular_function	nickel cation binding
M	0016491	molecular_function	oxidoreductase activity
M	0019645	biological_process	anaerobic electron transport chain
M	0030288	cellular_component	outer membrane-bounded periplasmic space
M	0033748	molecular_function	hydrogenase (acceptor) activity
M	0044569	cellular_component	[Ni-Fe] hydrogenase complex
M	0046872	molecular_function	metal ion binding
M	0098567	cellular_component	periplasmic side of plasma membrane
M	1902421	biological_process	hydrogen metabolic process
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	0009267	biological_process	cellular response to starvation
S	0009375	cellular_component	ferredoxin hydrogenase complex
S	0016020	cellular_component	membrane
S	0016491	molecular_function	oxidoreductase activity
S	0019645	biological_process	anaerobic electron transport chain
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
S	0098567	cellular_component	periplasmic side of plasma membrane
S	1902421	biological_process	hydrogen metabolic process
T	0005515	molecular_function	protein binding
T	0005886	cellular_component	plasma membrane
T	0008901	molecular_function	ferredoxin hydrogenase activity
T	0009055	molecular_function	electron transfer activity
T	0009061	biological_process	anaerobic respiration
T	0009267	biological_process	cellular response to starvation
T	0009375	cellular_component	ferredoxin hydrogenase complex
T	0016020	cellular_component	membrane
T	0016491	molecular_function	oxidoreductase activity
T	0019645	biological_process	anaerobic electron transport chain
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
T	0098567	cellular_component	periplasmic side of plasma membrane
T	1902421	biological_process	hydrogen metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue SF4 S 401

Chain	Residue
S	HIS187
S	CYS190
S	ARG192
S	ARG193
S	CYS215
S	LEU216
S	CYS221

site_id	AC2
Number of Residues	9
Details	binding site for residue F3S S 402

Chain	Residue
S	ASN228
S	CYS230
S	TRP235
S	PRO242
S	CYS249
S	LEU250
S	CYS252
L	LYS226
S	THR226

site_id	AC3
Number of Residues	8
Details	binding site for residue SF3 S 403

Chain	Residue
S	GLU16
S	CYS17
S	CYS19
S	CYS20
S	THR114
S	CYS115
S	CYS120
S	CYS149

site_id	AC4
Number of Residues	5
Details	binding site for residue CL S 404

Chain	Residue
S	TRP118
S	CYS120
S	GLY256
S	HOH621
S	HOH643

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 S 405

Chain	Residue
S	LYS218
S	ARG266
S	HOH534

site_id	AC6
Number of Residues	13
Details	binding site for residue EJ2 L 601

Chain	Residue
L	CYS76
L	CYS79
L	VAL82
L	HIS83
L	ALA507
L	PRO508
L	ARG509
L	LEU512
L	VAL530
L	PRO531
L	THR532
L	CYS576
L	CYS579

site_id	AC7
Number of Residues	6
Details	binding site for residue MG L 602

Chain	Residue
L	GLU57
L	CYS528
L	HIS582
L	HOH711
L	HOH725
L	HOH726

site_id	AC8
Number of Residues	6
Details	binding site for residue SF4 T 401

Chain	Residue
T	HIS187
T	CYS190
T	ARG193
T	CYS215
T	LEU216
T	CYS221

site_id	AC9
Number of Residues	9
Details	binding site for residue F3S T 402

Chain	Residue
M	LYS226
T	THR226
T	ASN228
T	CYS230
T	TRP235
T	PRO242
T	CYS249
T	LEU250
T	CYS252

site_id	AD1
Number of Residues	9
Details	binding site for residue SF3 T 403

Chain	Residue
T	GLU16
T	CYS17
T	CYS19
T	CYS20
T	THR114
T	CYS115
T	CYS120
T	GLY148
T	CYS149

site_id	AD2
Number of Residues	4
Details	binding site for residue CL T 404

Chain	Residue
T	TRP118
T	CYS120
T	GLY256
T	HOH631

site_id	AD3
Number of Residues	4
Details	binding site for residue SO4 M 601

Chain	Residue
M	ASN481
M	LEU482
M	ALA483
T	ARG211

site_id	AD4
Number of Residues	13
Details	binding site for residue EJ2 M 602

Chain	Residue
M	CYS76
M	CYS79
M	VAL82
M	HIS83
M	ALA507
M	PRO508
M	ARG509
M	LEU512
M	VAL530
M	PRO531
M	THR532
M	CYS576
M	CYS579

site_id	AD5
Number of Residues	6
Details	binding site for residue MG M 603

Chain	Residue
M	HOH716
M	HOH719
M	HOH720
M	GLU57
M	CYS528
M	HIS582

site_id	AD6
Number of Residues	13
Details	binding site for residue CXS M 604

Chain	Residue
L	LYS489
L	THR494
L	HOH904
L	HOH1203
M	LEU135
M	PHE182
M	ASN184
M	GLY185
M	TRP187
M	ILE559
M	GLN562
M	HOH891
M	HOH1064

site_id	AD7
Number of Residues	4
Details	binding site for residue LI M 605

Chain	Residue
L	HOH966
M	ASN184
M	HOH1062
T	HOH589

site_id	AD8
Number of Residues	4
Details	binding site for residue LI M 606

Chain	Residue
M	HOH772
M	HOH813
M	HOH944
M	HOH1074

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	ARG54-CYS79

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	PHE573-HIS582

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P21853","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)