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5OIU

Crystal structure of PilF type IV pilus assembly ATPase from Thermus thermophilus

Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ATP A 501
ChainResidue
ALYS123
ALEU287
AARG338
AALA340
AMG502
AHOH601
AHOH619
AHOH634
AHOH636
AHOH638
ALEU134
ATHR161
AGLY162
ASER163
AGLY164
ALYS165
ASER166
APHE167

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
ASER166
AGLU191
AATP501
AHOH601
AHOH634

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
ACYS292
ACYS295
ACYS327
ACYS330

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 504
ChainResidue
ASER163
ALEU287

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 505
ChainResidue
ATHR111
AVAL112
FTHR200
FGLN201

site_idAC6
Number of Residues17
Detailsbinding site for residue ATP B 501
ChainResidue
BLYS123
BLEU134
BTHR161
BGLY162
BSER163
BGLY164
BLYS165
BSER166
BPHE167
BLEU287
BARG338
BMG502
BHOH604
BHOH606
BHOH629
BHOH633
BHOH650

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BSER166
BATP501
BHOH604
BHOH606
BHOH629

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 503
ChainResidue
BCYS292
BCYS295
BCYS327
BCYS330

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 504
ChainResidue
BGLY162
BSER163
BLEU287

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 505
ChainResidue
BTHR111
BVAL112
EGLN201

site_idAD2
Number of Residues15
Detailsbinding site for residue ATP C 501
ChainResidue
CARG92
CTHR161
CGLY162
CSER163
CGLY164
CLYS165
CSER166
CPHE167
CLEU287
CARG338
CALA340
CMG502
CHOH605
CHOH609
CHOH617

site_idAD3
Number of Residues5
Detailsbinding site for residue MG C 502
ChainResidue
CSER166
CATP501
CHOH605
CHOH609
CHOH617

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN C 503
ChainResidue
CCYS292
CCYS295
CCYS327
CCYS330

site_idAD5
Number of Residues3
Detailsbinding site for residue CL C 504
ChainResidue
BGLN201
CTHR111
CVAL112

site_idAD6
Number of Residues2
Detailsbinding site for residue CL C 505
ChainResidue
BLYS323
CSER60

site_idAD7
Number of Residues2
Detailsbinding site for residue CL C 506
ChainResidue
CSER163
CLEU287

site_idAD8
Number of Residues16
Detailsbinding site for residue ATP D 501
ChainResidue
DGLY162
DSER163
DGLY164
DLYS165
DSER166
DPHE167
DLEU287
DARG338
DMG502
DHOH601
DHOH605
DHOH610
DHOH618
DARG92
DALA125
DTHR161

site_idAD9
Number of Residues5
Detailsbinding site for residue MG D 502
ChainResidue
DSER166
DATP501
DHOH601
DHOH610
DHOH618

site_idAE1
Number of Residues4
Detailsbinding site for residue ZN D 503
ChainResidue
DCYS292
DCYS295
DCYS327
DCYS330

site_idAE2
Number of Residues3
Detailsbinding site for residue CL D 504
ChainResidue
AGLN201
DTHR111
DVAL112

site_idAE3
Number of Residues1
Detailsbinding site for residue CL D 505
ChainResidue
ALYS323

site_idAE4
Number of Residues1
Detailsbinding site for residue CL D 506
ChainResidue
DLEU287

site_idAE5
Number of Residues15
Detailsbinding site for residue ATP E 501
ChainResidue
ELYS123
ELEU134
ETHR161
EGLY162
ESER163
EGLY164
ELYS165
ESER166
EPHE167
ELEU287
EARG338
EMG502
EHOH601
EHOH621
EHOH640

site_idAE6
Number of Residues4
Detailsbinding site for residue MG E 502
ChainResidue
ESER166
EGLU191
EATP501
EHOH601

site_idAE7
Number of Residues4
Detailsbinding site for residue ZN E 503
ChainResidue
ECYS292
ECYS295
ECYS327
ECYS330

site_idAE8
Number of Residues2
Detailsbinding site for residue CL E 504
ChainResidue
ESER163
ELEU287

site_idAE9
Number of Residues16
Detailsbinding site for residue ATP F 501
ChainResidue
FLYS123
FLEU134
FTHR161
FGLY162
FSER163
FGLY164
FLYS165
FSER166
FPHE167
FLEU287
FARG338
FMG502
FHOH603
FHOH604
FHOH616
FHOH621

site_idAF1
Number of Residues5
Detailsbinding site for residue MG F 502
ChainResidue
FSER166
FATP501
FHOH603
FHOH604
FHOH621

site_idAF2
Number of Residues4
Detailsbinding site for residue ZN F 503
ChainResidue
FCYS292
FCYS295
FCYS327
FCYS330

site_idAF3
Number of Residues3
Detailsbinding site for residue CL F 504
ChainResidue
FSER163
FLEU287
FARG397

Functional Information from PROSITE/UniProt
site_idPS00662
Number of Residues15
DetailsT2SP_E Bacterial type II secretion system protein E signature. LRqdPDiIMVGEIRD
ChainResidueDetails
ALEU218-ASP232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:27667690, ECO:0007744|PDB:5IT5
ChainResidueDetails
BCYS292
BCYS295
BCYS327
BCYS330
CGLY162
CCYS292
CCYS295
CCYS327
CCYS330
DGLY162
DCYS292
DCYS295
DCYS327
DCYS330
EGLY162
ECYS292
ECYS295
ECYS327
ECYS330
FGLY162
FCYS292
FCYS295
FCYS327
FCYS330
AGLY162
ACYS292
ACYS295
ACYS327
ACYS330
BGLY162

221051

PDB entries from 2024-06-12

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