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4CI0

Electron cryo-microscopy of F420-reducing NiFe hydrogenase Frh

Functional Information from GO Data
ChainGOidnamespacecontents
A0008901molecular_functionferredoxin hydrogenase activity
A0016151molecular_functionnickel cation binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050454molecular_functioncoenzyme F420 hydrogenase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0051536molecular_functioniron-sulfur cluster binding
B0016151molecular_functionnickel cation binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050454molecular_functioncoenzyme F420 hydrogenase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0000166molecular_functionnucleotide binding
C0016151molecular_functionnickel cation binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0050454molecular_functioncoenzyme F420 hydrogenase activity
C0050660molecular_functionflavin adenine dinucleotide binding
C0051536molecular_functioniron-sulfur cluster binding
C0051539molecular_function4 iron, 4 sulfur cluster binding
C0052592molecular_functionoxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 1387
ChainResidue
ACYS66
APRO350
ACYS383
ANI1388

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 1388
ChainResidue
ACYS63
ACYS66
ACYS380
ACYS383
AFE1387

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE2 A 1389
ChainResidue
AGLU44
AALA347
AHIS386

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 B 1274
ChainResidue
BGLY56
BCYS57
BTHR58
BGLY59
BASP60
BGLY130
BSER131
BCYS132
BCYS171

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 B 1275
ChainResidue
BALA229
BCYS230
BTHR232
BLEU235
BCYS249
BILE250
BCYS252
BGLY253
BCYS255

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SF4 B 1276
ChainResidue
BCYS220
BILE221
BGLY222
BCYS223
BGLY224
BTHR225
BCYS226
BMET237
BPRO242
BCYS259
BPRO260

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 1277
ChainResidue
BCYS206
BCYS208

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SF4 C 1282
ChainResidue
BILE221
CILE102
CPRO103
CCYS104
CCYS134
CMET135
CGLU136
CASN137
CCYS192
CCYS195
CLYS261

site_idAC9
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD C 1283
ChainResidue
CALA23
CGLN24
CASP25
CGLY26
CGLY27
CILE28
CVAL29
CTHR30
CVAL47
CALA48
CALA72
CGLY73
CTHR74
CLYS75
CTYR76
CTHR77
CASN81
CILE102
CGLN105
CILE132
CTYR133
CCYS134
CMET135
CASN137
CTYR198
CTHR207
CGLY208
CSER209
CVAL210

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiKCGiCYvQCP
ChainResidueDetails
BCYS249-PRO260

site_idPS00507
Number of Residues26
DetailsNI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEkmvtgkapetapvmvQRiCGVC
ChainResidueDetails
AARG41-CYS66

site_idPS00508
Number of Residues10
DetailsNI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. YDPCLSCat.H
ChainResidueDetails
ATYR377-HIS386

247536

PDB entries from 2026-01-14

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