1CC1

CRYSTAL STRUCTURE OF A REDUCED, ACTIVE FORM OF THE NI-FE-SE HYDROGENASE FROM DESULFOMICROBIUM BACULATUM

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	0033748	molecular_function	hydrogenase (acceptor) activity
L	0042597	cellular_component	periplasmic space
L	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	0042597	cellular_component	periplasmic space
S	0044569	cellular_component	[Ni-Fe] hydrogenase complex
S	0046872	molecular_function	metal ion binding
S	0051536	molecular_function	iron-sulfur cluster binding
S	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NI L 500

Chain	Residue
L	CYS495
L	FCO499
L	CYS70
L	CYS73
L	SEC492

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE2 L 501

Chain	Residue
L	GLU51
L	ILE444
L	HIS498
L	HOH519
L	HOH523
L	HOH541

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 S 284

Chain	Residue
S	HIS208
S	CYS211
S	TYR213
S	LEU214
S	CYS231
S	LYS232
S	CYS237
S	VAL259

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site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 S 285

Chain	Residue
L	ARG185
L	GLN190
S	THR242
S	CYS246
S	TRP251
S	CYS258
S	CYS264
S	ILE265
S	CYS267

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site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 S 286

Chain	Residue
L	ARG68
L	HIS188
S	CYS18
S	CYS21
S	GLY124
S	THR125
S	CYS126
S	GLY163
S	CYS164
S	PRO165

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site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FCO L 499

Chain	Residue
L	CYS73
L	HIS77
L	ALA423
L	PRO424
L	ARG425
L	LEU428
L	ALA447
L	THR448
L	SEC492
L	CYS495
L	NI500

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site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE H2S L 502

Chain	Residue
L	CYS73
L	THR75
L	ALA76
L	PHE105
L	ASN108
L	PRO424

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site_id	ACT
Number of Residues	6
Details	NI-FE ACTIVE SITE.

Chain	Residue
L	CYS70
L	CYS73
L	SEC492
L	CYS495
L	FCO499
L	NI500

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	ARG48-CYS73

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

Chain	Residue	Details
L	TYR489-HIS498

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
L	GLU51
S	CYS258
S	CYS264
S	CYS267
L	CYS70
L	CYS73
L	ILE444
L	SEC492
L	CYS495
L	HIS498
S	CYS237
S	CYS246

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 10378275

Chain	Residue	Details
S	THR19
L	CSE492
L	GLU23

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site_id	MCSA1
Number of Residues	7
Details	M-CSA 443

Chain	Residue	Details
L	GLU23	proton shuttle (general acid/base)
S	CYS258	metal ligand
S	CYS264	metal ligand
S	CYS267	metal ligand
L	CYS70	metal ligand
L	CYS73	metal ligand
L	HIS77	proton shuttle (general acid/base)
L	ARG425	electrostatic stabiliser
L	SEC492	activator, metal ligand
L	CYS495	metal ligand
S	CYS237	metal ligand
S	CYS246	metal ligand

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