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5BN3

Structure of a unique ATP synthase NeqA-NeqB in complex with ADP from Nanoarcheaum equitans

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006754biological_processATP biosynthetic process
A0042777biological_processproton motive force-driven plasma membrane ATP synthesis
A0046034biological_processATP metabolic process
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ADP A 601
ChainResidue
AGLY226
AALA493
APHE494
AMG609
AHOH741
AHOH753
AHOH774
AHOH819
AHOH833
BARG326
ASER227
AGLY228
ALYS229
ATHR230
AVAL231
ATYR414
AGLN491
AASP492

site_idAC2
Number of Residues6
Detailsbinding site for residue DIO A 602
ChainResidue
APHE449
AGOL606
AHOH761
BHIS310
BSER311
BASN313

site_idAC3
Number of Residues6
Detailsbinding site for residue DIO A 603
ChainResidue
AASP269
ATHR272
ALYS274
APRO275
ATYR278
AARG279

site_idAC4
Number of Residues5
Detailsbinding site for residue DIO A 604
ChainResidue
AASP405
ALYS407
ALEU408
AASN418
ATYR419

site_idAC5
Number of Residues7
Detailsbinding site for residue DIO A 605
ChainResidue
AGLN392
AILE421
AHOH722
AHOH779
BPRO136
BPRO283
BGLN307

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 606
ChainResidue
APHE211
ASER422
ATYR423
ATHR424
APHE449
ADIO602
BHIS310

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL A 607
ChainResidue
AGLY226
AALA409
ATYR414
AHOH796
AHOH822
BLEU321
BHOH673

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 608
ChainResidue
AASN197
ALYS215
ASER314
AARG362
ASER372
AHOH706

site_idAC9
Number of Residues6
Detailsbinding site for residue MG A 609
ChainResidue
ATHR230
AADP601
AHOH727
AHOH741
AHOH753
AHOH849

site_idAD1
Number of Residues3
Detailsbinding site for residue MG A 610
ChainResidue
AVAL315
ASER372
ATHR374

site_idAD2
Number of Residues3
Detailsbinding site for residue DIO B 501
ChainResidue
BSER333
BLYS334
BHOH613

site_idAD3
Number of Residues4
Detailsbinding site for residue DIO B 502
ChainResidue
BTYR112
BGLY331
BSER333
BHIS336

site_idAD4
Number of Residues4
Detailsbinding site for residue DIO B 503
ChainResidue
BSER66
BGLU67
BTYR212
BLYS217

site_idAD5
Number of Residues1
Detailsbinding site for residue DIO B 504
ChainResidue
BLYS243

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL B 505
ChainResidue
AARG412
AHOH733
BALA121
BHIS122
BLEU324
BSER325
BILE344

site_idAD7
Number of Residues2
Detailsbinding site for residue GOL B 506
ChainResidue
BSER366
BLYS367

site_idAD8
Number of Residues6
Detailsbinding site for residue GOL B 507
ChainResidue
BARG249
BTHR288
BHIS289
BVAL290
BHOH604
BHOH674

site_idAD9
Number of Residues8
Detailsbinding site for residue GOL B 508
ChainResidue
BASN95
BGLY96
BLEU97
BSER261
BARG265
BHOH601
BHOH727
AASN288

site_idAE1
Number of Residues1
Detailsbinding site for residue MG B 510
ChainResidue
BTYR102

site_idAE2
Number of Residues1
Detailsbinding site for residue MG B 511
ChainResidue
BASP93

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 B 512
ChainResidue
BSER306
BGLN307
BASP308
BHOH605
BHOH612
BHOH621
BHOH704

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00309
ChainResidueDetails
AGLY223

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PDB entries from 2024-07-10

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