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4XKR

Crystal structure of NikA from Staphylococcus aureus in complex with Ni-(L-His)(2-methyl-thiazolidine dicarboxylate) (co-crystallization with Ni(II) and CDdeltaHis medium supernatant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0015675biological_processnickel cation transport
A0015833biological_processpeptide transport
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055085biological_processtransmembrane transport
A1904680molecular_functionpeptide transmembrane transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue NI A 501
ChainResidue
AHIS502
A41K503

site_idAC2
Number of Residues11
Detailsbinding site for residue HIS A 502
ChainResidue
ANI501
A41K503
ANA523
AHOH773
ALEU17
AARG234
ATYR322
AARG325
AGLU355
ATYR369
ASER370

site_idAC3
Number of Residues15
Detailsbinding site for residue 41K A 503
ChainResidue
AASP28
APHE134
AARG234
ATYR369
ASER370
APHE371
AGLY372
AILE393
ANI501
AHIS502
ANA523
AHOH752
AHOH784
AHOH836
AHOH846

site_idAC4
Number of Residues12
Detailsbinding site for residue EPE A 504
ChainResidue
AILE48
AGLU49
ALYS50
ATYR56
ATYR101
ALYS389
AASP390
AASP404
AGOL508
AHOH645
AHOH676
AHOH961

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 505
ChainResidue
ALYS159
ALYS318
ALYS349
ATYR357
AHOH610
AHOH986

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL A 506
ChainResidue
ALYS32
ALYS456
AGLY461
AILE462
ATYR463
AHOH759
AHOH786
AHOH840
AHOH990

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 507
ChainResidue
AGLU83
AALA110
AGLN295
AILE297
AASP338
AGOL521
AHOH625
AHOH644
AHOH668

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 508
ChainResidue
ATYR101
AASN384
ALYS388
ALYS389
AEPE504
AHOH845

site_idAC9
Number of Residues8
Detailsbinding site for residue GOL A 509
ChainResidue
AASP260
AGLY263
AILE264
AHIS267
AVAL334
AHOH800
AHOH815
AHOH1046

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 510
ChainResidue
AGLU90
ASER106
AILE108
AHOH673
AHOH818

site_idAD2
Number of Residues10
Detailsbinding site for residue GOL A 511
ChainResidue
ASER55
AGLU67
AARG252
ATYR398
AASN399
AASN400
AASP433
AGOL518
AHOH602
AHOH612

site_idAD3
Number of Residues10
Detailsbinding site for residue GOL A 512
ChainResidue
ASER431
AHOH742
AHOH772
AHOH798
AASP256
AARG261
ATHR277
APRO290
ALYS291
ATHR293

site_idAD4
Number of Residues8
Detailsbinding site for residue GOL A 513
ChainResidue
AGLN58
AASN60
AASP61
ATHR63
ATHR119
AALA122
ATYR123
AHOH771

site_idAD5
Number of Residues7
Detailsbinding site for residue GOL A 514
ChainResidue
ATHR149
ALYS159
AILE348
ALYS349
ASER350
AHOH619
AHOH666

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL A 515
ChainResidue
ATYR463
AHOH749
AHOH826
AHOH855
AHOH869
AHOH889
AHOH910

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL A 516
ChainResidue
ALYS226
ALYS453
AASN454
ATYR455
AHOH1007

site_idAD8
Number of Residues4
Detailsbinding site for residue GOL A 517
ChainResidue
ALYS143
AVAL351
AASP352
AASP353

site_idAD9
Number of Residues10
Detailsbinding site for residue GOL A 518
ChainResidue
ALYS114
AHIS242
ALYS245
AMET247
ATHR248
AARG252
AGOL511
AHOH602
AHOH675
AHOH681

site_idAE1
Number of Residues7
Detailsbinding site for residue GOL A 519
ChainResidue
ALYS54
ALYS69
AASP70
AASN71
AASN402
AHOH632
AHOH957

site_idAE2
Number of Residues6
Detailsbinding site for residue GOL A 520
ChainResidue
ATHR109
AALA110
ALYS114
ALEU115
ATHR116
ALYS245

site_idAE3
Number of Residues7
Detailsbinding site for residue GOL A 521
ChainResidue
AGLU83
ALYS86
ATHR109
AALA110
AGLU298
ALYS341
AGOL507

site_idAE4
Number of Residues8
Detailsbinding site for residue GOL A 522
ChainResidue
APHE134
AALA392
ALYS395
ANA523
AHOH820
AHOH893
AHOH940
AHOH969

site_idAE5
Number of Residues5
Detailsbinding site for residue NA A 523
ChainResidue
AGLU355
AHIS502
A41K503
AGOL522
AHOH813

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLIPID: S-diacylglycerol cysteine => ECO:0000255|PROSITE-ProRule:PRU00303
ChainResidueDetails
ACYS1

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PDB entries from 2024-07-17

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