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5T5M

TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRIGONAL FORM AT 2.5 A.

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
B0003954molecular_functionNADH dehydrogenase activity
B0015948biological_processmethanogenesis
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0018493molecular_functionformylmethanofuran dehydrogenase activity
B0022904biological_processrespiratory electron transport chain
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0015948biological_processmethanogenesis
C0016491molecular_functionoxidoreductase activity
C0018493molecular_functionformylmethanofuran dehydrogenase activity
C0019386biological_processmethanogenesis, from carbon dioxide
C0046914molecular_functiontransition metal ion binding
D0016491molecular_functionoxidoreductase activity
D0043546molecular_functionmolybdopterin cofactor binding
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
F0051536molecular_functioniron-sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
G0016491molecular_functionoxidoreductase activity
G0046872molecular_functionmetal ion binding
G0051536molecular_functioniron-sulfur cluster binding
G0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 601
ChainResidue
AVAL340
ATHR344
AHOH729
AHOH738
BGLU138

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 602
ChainResidue
AHOH720
AKCX178
AHIS231
AHIS271
AZN603

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 603
ChainResidue
AHIS57
AHIS59
AKCX178
AASP385
AZN602
AHOH720

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 604
ChainResidue
AARG69
AARG72
ASER76
AHOH726
AHOH757
BGLY305

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 605
ChainResidue
ATRP190
AGLY191

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL A 606
ChainResidue
ALYS77
CGLU82

site_idAC7
Number of Residues3
Detailsbinding site for residue K B 501
ChainResidue
BSER40
BVAL43
DGLU18

site_idAC8
Number of Residues4
Detailsbinding site for residue SF4 B 502
ChainResidue
BCYS9
BCYS12
BCYS16
BCYS35

site_idAC9
Number of Residues4
Detailsbinding site for residue W B 503
ChainResidue
BCYS118
BMGD504
BMGD505
BH2S506

site_idAD1
Number of Residues34
Detailsbinding site for residue MGD B 504
ChainResidue
BLYS41
BCYS91
BTHR114
BVAL117
BCYS118
BMET254
BHIS258
BHIS290
BALA342
BSER343
BASP344
BHIS348
BILE365
BGLU366
BPRO367
BHIS368
BTHR370
BPRO382
BILE384
BVAL385
BASP414
BW503
BMGD505
BH2S506
BHOH603
BHOH612
BHOH623
DTHR7
DARG9
DLYS21
DMET80
DASN85
DPHE100
DLYS101

site_idAD2
Number of Residues37
Detailsbinding site for residue MGD B 505
ChainResidue
DGLY8
DARG9
DTHR10
DGLN13
DGLY14
DILE17
DMET80
DLYS101
DASN102
BPHE11
BILE37
BCYS118
BGLY150
BCYS151
BASN152
BHIS155
BALA156
BVAL184
BASP185
BPRO186
BARG187
BTHR189
BPHE203
BASP204
BASP206
BGLY253
BMET254
BGLY255
BSER259
BGLY289
BHIS290
BW503
BMGD504
BH2S506
BHOH631
BHOH637
DASN6

site_idAD3
Number of Residues6
Detailsbinding site for residue H2S B 506
ChainResidue
BTHR114
BCYS118
BHIS290
BW503
BMGD504
BMGD505

site_idAD4
Number of Residues7
Detailsbinding site for residue MG C 301
ChainResidue
BASP128
BHOH609
BHOH654
CSER139
CTYR140
CGLY142
CASP143

site_idAD5
Number of Residues2
Detailsbinding site for residue GOL D 201
ChainResidue
DARG89
DTYR91

site_idAD6
Number of Residues6
Detailsbinding site for residue SF4 F 501
ChainResidue
FCYS154
FTYR156
FCYS157
FGLY158
FCYS160
FCYS204

site_idAD7
Number of Residues5
Detailsbinding site for residue SF4 F 502
ChainResidue
FCYS164
FCYS194
FCYS197
FGLY198
FCYS200

site_idAD8
Number of Residues4
Detailsbinding site for residue SF4 F 503
ChainResidue
FCYS281
FCYS308
FCYS311
FCYS314

site_idAD9
Number of Residues6
Detailsbinding site for residue SF4 F 504
ChainResidue
FCYS271
FCYS274
FGLU275
FCYS277
FCYS318
FILE323

site_idAE1
Number of Residues6
Detailsbinding site for residue SF4 F 505
ChainResidue
FLEU24
FCYS41
FCYS71
FCYS74
FGLY75
FCYS77

site_idAE2
Number of Residues6
Detailsbinding site for residue SF4 F 506
ChainResidue
FCYS31
FCYS34
FGLY35
FCYS37
FCYS81
FPHE83

site_idAE3
Number of Residues8
Detailsbinding site for residue SF4 F 507
ChainResidue
FCYS125
FILE130
FCYS239
FVAL240
FASN241
FCYS242
FGLY243
FCYS245

site_idAE4
Number of Residues6
Detailsbinding site for residue SF4 F 508
ChainResidue
FCYS115
FILE116
FCYS118
FLYS119
FCYS121
FCYS249

site_idAE5
Number of Residues6
Detailsbinding site for residue SF4 G 200
ChainResidue
GCYS12
GHIS13
GCYS15
GGLY16
GCYS18
GCYS71

site_idAE6
Number of Residues5
Detailsbinding site for residue SF4 G 201
ChainResidue
GCYS22
GCYS61
GCYS64
GGLY65
GCYS67

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CaVCGlCGeICP
ChainResidueDetails
FCYS31-PRO42
GCYS61-PRO72
FCYS71-PRO82
FCYS115-PRO126
FCYS154-PRO165
FCYS194-PRO205
FCYS239-PRO250
FCYS271-PRO282
FCYS308-PRO319
GCYS12-PRO23

237735

PDB entries from 2025-06-18

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