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6ZHV

Crystal structure of OmpF porin soaked in ciprofloxacin metaloantibiotic

Functional Information from GO Data
ChainGOidnamespacecontents
A0009279cellular_componentcell outer membrane
A0015288molecular_functionporin activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0009279cellular_componentcell outer membrane
B0015288molecular_functionporin activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0009279cellular_componentcell outer membrane
C0015288molecular_functionporin activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
BASN229
BASN258
BASN274
BHOH539
BHOH546
BHOH552

site_idAC2
Number of Residues5
Detailsbinding site for residue NA B 402
ChainResidue
BALA97
BHOH532
ALYS102
ATHR103
AHOH539

site_idAC3
Number of Residues5
Detailsbinding site for residue NA B 403
ChainResidue
ATYR85
AHOH541
BTYR85
BHOH544
CHOH536

site_idAC4
Number of Residues4
Detailsbinding site for residue NA B 404
ChainResidue
BASN338
BILE340
BSER350
BHOH550

site_idAC5
Number of Residues4
Detailsbinding site for residue NA B 405
ChainResidue
BGLU223
BGLN225
BGLY228
BHOH553

site_idAC6
Number of Residues4
Detailsbinding site for residue NA B 406
ChainResidue
BARG218
BGLN222
BLEU227
BGLY228

site_idAC7
Number of Residues6
Detailsbinding site for residue QLB B 407
ChainResidue
ATYR120
ATYR179
ALEU180
BTHR331
BVAL333
BVAL356

site_idAC8
Number of Residues4
Detailsbinding site for residue MG A 401
ChainResidue
AASN229
AASN258
AASN274
AHOH542

site_idAC9
Number of Residues3
Detailsbinding site for residue NA A 402
ChainResidue
AGLU223
AGLN225
AGLY228

site_idAD1
Number of Residues3
Detailsbinding site for residue NA A 403
ChainResidue
AASP312
AASP341
AHOH550

site_idAD2
Number of Residues4
Detailsbinding site for residue NA A 404
ChainResidue
AMET329
ASER330
AGLN361
AHOH538

site_idAD3
Number of Residues5
Detailsbinding site for residue NA A 405
ChainResidue
AARG218
AGLN222
ALEU227
AGLY228
APHE272

site_idAD4
Number of Residues4
Detailsbinding site for residue QLB A 406
ChainResidue
ATHR331
AVAL333
AVAL356
CPHE118

site_idAD5
Number of Residues8
Detailsbinding site for residue QLB A 407
ChainResidue
ALEU249
AALA250
ALEU281
AVAL282
AALA283
APHE317
AVAL319
BVAL279

site_idAD6
Number of Residues6
Detailsbinding site for residue MG C 401
ChainResidue
CASN229
CASN258
CASN274
CHOH549
CHOH550
CHOH559

site_idAD7
Number of Residues3
Detailsbinding site for residue NA C 402
ChainResidue
CGLU223
CGLN225
CGLY228

site_idAD8
Number of Residues3
Detailsbinding site for residue NA C 403
ChainResidue
CHOH503
CHOH551
CHOH552

site_idAD9
Number of Residues5
Detailsbinding site for residue NA C 404
ChainResidue
CARG218
CGLN222
CLEU227
CGLY228
CPHE272

site_idAE1
Number of Residues8
Detailsbinding site for residue QLB C 405
ChainResidue
CPHE166
CALA176
CVAL177
CGLY198
CSER199
CGLY211
CALA212
CPHE287

site_idAE2
Number of Residues6
Detailsbinding site for residue QLB C 406
ChainResidue
CVAL196
CTYR213
CALA215
CLYS232
CTYR285
CPHE287

site_idAE3
Number of Residues6
Detailsbinding site for residue QLB C 407
ChainResidue
BGLY195
BVAL196
CVAL356
BTYR179
BLEU180
BGLY181

site_idAE4
Number of Residues3
Detailsbinding site for residue QLB C 408
ChainResidue
CALA250
CLEU281
CILE295

Functional Information from PROSITE/UniProt
site_idPS00576
Number of Residues17
DetailsGRAM_NEG_PORIN General diffusion Gram-negative porins signature. FevGatYyFnKnmSTYV
ChainResidueDetails
BPHE317-VAL333

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues510
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
BALA23-LYS28
BGLY206-ASP217
BALA233-ALA244
BASN246-ARG257
BLYS275-PHE287
BGLY290-LYS303
BVAL314-PHE325
BASN328-ILE337
BTHR353-PHE362
AALA23-LYS28
AGLY30-PHE45
BGLY30-PHE45
ATHR61-ILE73
AASP76-GLN88
ALEU105-ALA113
AGLY116-ARG122
AGLY157-ASN163
AGLY172-GLY181
AASP194-TYR204
AGLY206-ASP217
AALA233-ALA244
AASN246-ARG257
BTHR61-ILE73
ALYS275-PHE287
AGLY290-LYS303
AVAL314-PHE325
AASN328-ILE337
ATHR353-PHE362
CALA23-LYS28
CGLY30-PHE45
CTHR61-ILE73
CASP76-GLN88
CLEU105-ALA113
BASP76-GLN88
CGLY116-ARG122
CGLY157-ASN163
CGLY172-GLY181
CASP194-TYR204
CGLY206-ASP217
CALA233-ALA244
CASN246-ARG257
CLYS275-PHE287
CGLY290-LYS303
CVAL314-PHE325
BLEU105-ALA113
CASN328-ILE337
CTHR353-PHE362
BGLY116-ARG122
BGLY157-ASN163
BGLY172-GLY181
BASP194-TYR204

site_idSWS_FT_FI2
Number of Residues42
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
BASP29
AASN74-SER75
AASP114-VAL115
ASER164-ASP171
AGLU205
AASN245
AASP288-PHE289
AASN326-LYS327
CASP29
CASN74-SER75
CASP114-VAL115
BASN74-SER75
CSER164-ASP171
CGLU205
CASN245
CASP288-PHE289
CASN326-LYS327
BASP114-VAL115
BSER164-ASP171
BGLU205
BASN245
BASP288-PHE289
BASN326-LYS327
AASP29

site_idSWS_FT_FI3
Number of Residues378
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
BSER46-MET60
AGLY89-ARG104
AASN123-GLY156
ALYS182-GLY193
AARG218-LYS232
AASN258-ASN274
AASP304-LEU313
AASN338-ASP352
CSER46-MET60
CGLY89-ARG104
CASN123-GLY156
BGLY89-ARG104
CLYS182-GLY193
CARG218-LYS232
CASN258-ASN274
CASP304-LEU313
CASN338-ASP352
BASN123-GLY156
BLYS182-GLY193
BARG218-LYS232
BASN258-ASN274
BASP304-LEU313
BASN338-ASP352
ASER46-MET60

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PDB entries from 2024-07-24

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