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2J1N

osmoporin OmpC

Functional Information from GO Data
ChainGOidnamespacecontents
A0001618molecular_functionvirus receptor activity
A0005515molecular_functionprotein binding
A0006811biological_processmonoatomic ion transport
A0006974biological_processDNA damage response
A0009279cellular_componentcell outer membrane
A0015288molecular_functionporin activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0046718biological_processsymbiont entry into host cell
A0046813biological_processreceptor-mediated virion attachment to host cell
A0046872molecular_functionmetal ion binding
A0046930cellular_componentpore complex
A0120010biological_processintermembrane phospholipid transfer
B0001618molecular_functionvirus receptor activity
B0005515molecular_functionprotein binding
B0006811biological_processmonoatomic ion transport
B0006974biological_processDNA damage response
B0009279cellular_componentcell outer membrane
B0015288molecular_functionporin activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0046718biological_processsymbiont entry into host cell
B0046813biological_processreceptor-mediated virion attachment to host cell
B0046872molecular_functionmetal ion binding
B0046930cellular_componentpore complex
B0120010biological_processintermembrane phospholipid transfer
C0001618molecular_functionvirus receptor activity
C0005515molecular_functionprotein binding
C0006811biological_processmonoatomic ion transport
C0006974biological_processDNA damage response
C0009279cellular_componentcell outer membrane
C0015288molecular_functionporin activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0042802molecular_functionidentical protein binding
C0046718biological_processsymbiont entry into host cell
C0046813biological_processreceptor-mediated virion attachment to host cell
C0046872molecular_functionmetal ion binding
C0046930cellular_componentpore complex
C0120010biological_processintermembrane phospholipid transfer
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A1347
ChainResidue
AASN319
ALEU321
ATHR334
AHOH2140
AHOH2148

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B1347
ChainResidue
BHOH2194
BASN319
BLEU321
BTHR334
BHOH2191

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B1348
ChainResidue
BTHR47
BASP48
CTHR47
CASP48

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B1349
ChainResidue
AASN69
BASN69
CASN69

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C1347
ChainResidue
CASN319
CLEU321
CTHR334
CHOH2189
CHOH2191
CHOH2202

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D12 C1348
ChainResidue
BVAL338
CTYR277
CGLN279
CD121350

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D12 C1349
ChainResidue
ATYR131
CGLY194
CGLY223
CGLY224

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE D12 C1350
ChainResidue
BLEU340
CPHE259
CD121348

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE D12 C1351
ChainResidue
ATYR149
CILE197
CTHR222

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE D12 C1352
ChainResidue
CLYS226
CTYR227
CVAL262
CALA276
CTYR277

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE D12 C1353
ChainResidue
CTYR94
CHOH2027

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D12 C1354
ChainResidue
CPHE23
CASN336
CILE337
CVAL338

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE D12 C1357
ChainResidue
AARG132

Functional Information from PROSITE/UniProt
site_idPS00576
Number of Residues17
DetailsGRAM_NEG_PORIN General diffusion Gram-negative porins signature. VdvGatYyFnKnmSTYV
ChainResidueDetails
AVAL298-VAL314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:16949612
ChainResidueDetails
AALA1-ASP12
BALA1-ASP12
BGLU43-GLY52
BLYS81-VAL85
BTHR134-GLY142
BASP187-GLY190
BASP228-ASN231
BGLN266-GLY270
BPHE306-ASN309
BPHE346
CALA1-ASP12
AGLU43-GLY52
CGLU43-GLY52
CLYS81-VAL85
CTHR134-GLY142
CASP187-GLY190
CASP228-ASN231
CGLN266-GLY270
CPHE306-ASN309
CPHE346
ALYS81-VAL85
ATHR134-GLY142
AASP187-GLY190
AASP228-ASN231
AGLN266-GLY270
APHE306-ASN309
APHE346

site_idSWS_FT_FI2
Number of Residues399
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
ALEU13-HIS21
ATYR221-TYR227
AILE232-THR239
ASER249-TYR265
ALEU271-LEU278
AVAL298-TYR305
AMET310-LYS317
AVAL338-GLN345
BLEU13-HIS21
BGLN33-GLY42
BTYR53-ASN63
AGLN33-GLY42
BSER71-LEU80
BGLY86-TYR94
BMET121-ASN133
BLEU143-GLN150
BVAL180-TYR186
BPHE191-SER198
BTYR221-TYR227
BILE232-THR239
BSER249-TYR265
BLEU271-LEU278
ATYR53-ASN63
BVAL298-TYR305
BMET310-LYS317
BVAL338-GLN345
CLEU13-HIS21
CGLN33-GLY42
CTYR53-ASN63
CSER71-LEU80
CGLY86-TYR94
CMET121-ASN133
CLEU143-GLN150
ASER71-LEU80
CVAL180-TYR186
CPHE191-SER198
CTYR221-TYR227
CILE232-THR239
CSER249-TYR265
CLEU271-LEU278
CVAL298-TYR305
CMET310-LYS317
CVAL338-GLN345
AGLY86-TYR94
AMET121-ASN133
ALEU143-GLN150
AVAL180-TYR186
APHE191-SER198

site_idSWS_FT_FI3
Number of Residues405
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:16949612
ChainResidueDetails
ATYR22-ASP32
BSER64-ASN70
BGLY95-PHE120
BGLY151-GLY179
BSER199-THR220
BGLN240-GLY248
BGLN279-TYR297
BILE318-ILE337
CTYR22-ASP32
CSER64-ASN70
CGLY95-PHE120
ASER64-ASN70
CGLY151-GLY179
CSER199-THR220
CGLN240-GLY248
CGLN279-TYR297
CILE318-ILE337
AGLY95-PHE120
AGLY151-GLY179
ASER199-THR220
AGLN240-GLY248
AGLN279-TYR297
AILE318-ILE337
BTYR22-ASP32

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0007744|PDB:2J1N
ChainResidueDetails
AASN319
ALEU321
ATHR334
BASN319
BLEU321
BTHR334
CASN319
CLEU321
CTHR334

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PDB entries from 2024-08-21

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