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4OMF

The F420-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member

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
B0000166molecular_functionnucleotide 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
B0052592molecular_functionoxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor
G0016151molecular_functionnickel cation binding
G0016491molecular_functionoxidoreductase activity
G0046872molecular_functionmetal ion binding
G0050454molecular_functioncoenzyme F420 hydrogenase activity
G0050660molecular_functionflavin adenine dinucleotide binding
G0051536molecular_functioniron-sulfur cluster binding
G0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 G 301
ChainResidue
AHIS150
GGLY56
GCYS57
GASP60
GSER131
GCYS132
GPHE138
GGLY170
GCYS171

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 G 302
ChainResidue
GGLY207
GCYS230
GTHR232
GLEU235
GLEU244
GCYS249
GILE250
GCYS252
GGLY253
GCYS255

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 G 303
ChainResidue
GCYS220
GILE221
GGLY222
GCYS223
GGLY224
GCYS226
GCYS259
GPRO260

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTZ G 304
ChainResidue
GCYS206
GCYS206
GCYS208
GCYS208
GLYS251
GHOH565

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AGLU233
AHOH666
AHOH707
GALA148
GHOH475

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NFU A 502
ChainResidue
ACYS63
ACYS66
AHIS70
AALA326
APRO327
AARG328
AASP331
AVAL349
APRO350
ATHR351
ACYS380
ACYS383

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AGLU44
AALA347
AHIS386
AHOH961
AHOH962
AHOH963

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 504
ChainResidue
AHOH601
AHOH925
AHOH926
AHOH959
AHOH965
AHOH966

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
AILE156
AARG308
AHOH683
AHOH699

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SF4 B 401
ChainResidue
BILE102
BPRO103
BCYS104
BCYS134
BMET135
BGLU136
BASN137
BCYS192
BCYS195
BLYS261
GILE221
GARG261

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BHOH501
BHOH570
BHOH626
BHOH660
BHOH694
BHOH695

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE KEN B 403
ChainResidue
BARG110
BGLN113
BILE126
BASP204

site_idBC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD B 405
ChainResidue
BGLY73
BTHR74
BLYS75
BTYR76
BTHR77
BSER79
BASN81
BTYR133
BCYS134
BMET135
BGLU136
BASN137
BTYR198
BGLY208
BSER209
BVAL210
BHOH507
BHOH514
BHOH591
BHOH619
BALA23
BGLN24
BASP25
BGLY26
BGLY27
BILE28
BVAL29
BTHR30
BVAL47
BALA48
BALA71

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiKCGiCYvQCP
ChainResidueDetails
GCYS249-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

218500

数据于2024-04-17公开中

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