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6WBM

Cryo-EM structure of human Pannexin 1 channel N255A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0006812biological_processmonoatomic cation transport
A0015267molecular_functionchannel activity
A0032732biological_processpositive regulation of interleukin-1 production
B0006812biological_processmonoatomic cation transport
B0015267molecular_functionchannel activity
B0032732biological_processpositive regulation of interleukin-1 production
C0006812biological_processmonoatomic cation transport
C0015267molecular_functionchannel activity
C0032732biological_processpositive regulation of interleukin-1 production
D0006812biological_processmonoatomic cation transport
D0015267molecular_functionchannel activity
D0032732biological_processpositive regulation of interleukin-1 production
E0006812biological_processmonoatomic cation transport
E0015267molecular_functionchannel activity
E0032732biological_processpositive regulation of interleukin-1 production
F0006812biological_processmonoatomic cation transport
F0015267molecular_functionchannel activity
F0032732biological_processpositive regulation of interleukin-1 production
G0006812biological_processmonoatomic cation transport
G0015267molecular_functionchannel activity
G0032732biological_processpositive regulation of interleukin-1 production
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PTY A 401
ChainResidue
AGLY99
AASN100
ALEU101
ATRP104
ALEU115
ACLR405
BILE279
BPTY402

site_idAC2
Number of Residues7
Detailsbinding site for residue PTY A 402
ChainResidue
ALEU237
ASER239
AGLN274
ALEU275
AVAL278
GPTY401
APHE235

site_idAC3
Number of Residues8
Detailsbinding site for residue 3PE A 403
ChainResidue
AMET37
ATYR293
AARG300
AGLU336
GPHE126
GPHE129
GSER215
GLEU219

site_idAC4
Number of Residues4
Detailsbinding site for residue DGA A 404
ChainResidue
ALEU17
AMET37
AILE41
GPHE129

site_idAC5
Number of Residues2
Detailsbinding site for residue CLR A 405
ChainResidue
ATYR230
APTY401

site_idAC6
Number of Residues2
Detailsbinding site for residue CLR A 406
ChainResidue
AILE229
ASER236

site_idAC7
Number of Residues4
Detailsbinding site for residue DGA A 407
ChainResidue
APHE129
BLEU17
BMET37
BILE41

site_idAC8
Number of Residues8
Detailsbinding site for residue PTY B 401
ChainResidue
BGLY99
BASN100
BLEU101
BTRP104
BLEU115
BCLR404
CILE279
CPTY402

site_idAC9
Number of Residues7
Detailsbinding site for residue PTY B 402
ChainResidue
APTY401
BPHE235
BLEU237
BSER239
BGLN274
BLEU275
BVAL278

site_idAD1
Number of Residues8
Detailsbinding site for residue 3PE B 403
ChainResidue
APHE126
APHE129
ASER215
ALEU219
BMET37
BTYR293
BARG300
BGLU336

site_idAD2
Number of Residues2
Detailsbinding site for residue CLR B 404
ChainResidue
BTYR230
BPTY401

site_idAD3
Number of Residues2
Detailsbinding site for residue CLR B 405
ChainResidue
BILE229
BSER236

site_idAD4
Number of Residues5
Detailsbinding site for residue DGA B 406
ChainResidue
BLEU125
BPHE129
CLEU17
CMET37
CILE41

site_idAD5
Number of Residues8
Detailsbinding site for residue PTY C 401
ChainResidue
CGLY99
CASN100
CLEU101
CTRP104
CLEU115
CCLR404
DILE279
DPTY402

site_idAD6
Number of Residues7
Detailsbinding site for residue PTY C 402
ChainResidue
BPTY401
CPHE235
CLEU237
CSER239
CGLN274
CLEU275
CVAL278

site_idAD7
Number of Residues8
Detailsbinding site for residue 3PE C 403
ChainResidue
BPHE126
BPHE129
BSER215
BLEU219
CMET37
CTYR293
CARG300
CGLU336

site_idAD8
Number of Residues2
Detailsbinding site for residue CLR C 404
ChainResidue
CTYR230
CPTY401

site_idAD9
Number of Residues2
Detailsbinding site for residue CLR C 405
ChainResidue
CILE229
CSER236

site_idAE1
Number of Residues5
Detailsbinding site for residue DGA C 406
ChainResidue
CLEU125
CPHE129
DLEU17
DMET37
DILE41

site_idAE2
Number of Residues8
Detailsbinding site for residue PTY D 401
ChainResidue
DGLY99
DASN100
DLEU101
DTRP104
DLEU115
DCLR404
EILE279
EPTY402

site_idAE3
Number of Residues7
Detailsbinding site for residue PTY D 402
ChainResidue
CPTY401
DPHE235
DLEU237
DSER239
DGLN274
DLEU275
DVAL278

site_idAE4
Number of Residues8
Detailsbinding site for residue 3PE D 403
ChainResidue
CPHE126
CPHE129
CSER215
CLEU219
DMET37
DTYR293
DARG300
DGLU336

site_idAE5
Number of Residues2
Detailsbinding site for residue CLR D 404
ChainResidue
DTYR230
DPTY401

site_idAE6
Number of Residues2
Detailsbinding site for residue CLR D 405
ChainResidue
DILE229
DSER236

site_idAE7
Number of Residues5
Detailsbinding site for residue DGA D 406
ChainResidue
DLEU125
DPHE129
ELEU17
EMET37
EILE41

site_idAE8
Number of Residues8
Detailsbinding site for residue PTY E 401
ChainResidue
EGLY99
EASN100
ELEU101
ETRP104
ELEU115
ECLR404
FILE279
FPTY402

site_idAE9
Number of Residues7
Detailsbinding site for residue PTY E 402
ChainResidue
DPTY401
EPHE235
ELEU237
ESER239
EGLN274
ELEU275
EVAL278

site_idAF1
Number of Residues8
Detailsbinding site for residue 3PE E 403
ChainResidue
DPHE126
DPHE129
DSER215
DLEU219
EMET37
ETYR293
EARG300
EGLU336

site_idAF2
Number of Residues2
Detailsbinding site for residue CLR E 404
ChainResidue
ETYR230
EPTY401

site_idAF3
Number of Residues2
Detailsbinding site for residue CLR E 405
ChainResidue
EILE229
ESER236

site_idAF4
Number of Residues5
Detailsbinding site for residue DGA E 406
ChainResidue
ELEU125
EPHE129
FLEU17
FMET37
FILE41

site_idAF5
Number of Residues8
Detailsbinding site for residue PTY F 401
ChainResidue
FGLY99
FASN100
FLEU101
FTRP104
FLEU115
FCLR404
GILE279
GPTY402

site_idAF6
Number of Residues7
Detailsbinding site for residue PTY F 402
ChainResidue
EPTY401
FPHE235
FLEU237
FSER239
FGLN274
FLEU275
FVAL278

site_idAF7
Number of Residues8
Detailsbinding site for residue 3PE F 403
ChainResidue
EPHE126
EPHE129
ESER215
ELEU219
FMET37
FTYR293
FARG300
FGLU336

site_idAF8
Number of Residues2
Detailsbinding site for residue CLR F 404
ChainResidue
FTYR230
FPTY401

site_idAF9
Number of Residues2
Detailsbinding site for residue CLR F 405
ChainResidue
FILE229
FSER236

site_idAG1
Number of Residues5
Detailsbinding site for residue DGA F 406
ChainResidue
FLEU125
FPHE129
GLEU17
GMET37
GILE41

site_idAG2
Number of Residues8
Detailsbinding site for residue PTY G 401
ChainResidue
AILE279
APTY402
GGLY99
GASN100
GLEU101
GTRP104
GLEU115
GCLR404

site_idAG3
Number of Residues7
Detailsbinding site for residue PTY G 402
ChainResidue
FPTY401
GPHE235
GLEU237
GSER239
GGLN274
GLEU275
GVAL278

site_idAG4
Number of Residues8
Detailsbinding site for residue 3PE G 403
ChainResidue
FPHE126
FPHE129
FSER215
FLEU219
GMET37
GTYR293
GARG300
GGLU336

site_idAG5
Number of Residues2
Detailsbinding site for residue CLR G 404
ChainResidue
GTYR230
GPTY401

site_idAG6
Number of Residues2
Detailsbinding site for residue CLR G 405
ChainResidue
GILE229
GSER236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues896
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-CYS40
EARG128-ARG217
FMET1-CYS40
FARG128-ARG217
GMET1-CYS40
GARG128-ARG217
AARG128-ARG217
BMET1-CYS40
BARG128-ARG217
CMET1-CYS40
CARG128-ARG217
DMET1-CYS40
DARG128-ARG217
EMET1-CYS40

site_idSWS_FT_FI2
Number of Residues560
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00351
ChainResidueDetails
AILE41-GLY61
CLYS107-TRP127
CLEU218-SER238
CLEU267-LEU287
DILE41-GLY61
DLYS107-TRP127
DLEU218-SER238
DLEU267-LEU287
EILE41-GLY61
ELYS107-TRP127
ELEU218-SER238
ALYS107-TRP127
ELEU267-LEU287
FILE41-GLY61
FLYS107-TRP127
FLEU218-SER238
FLEU267-LEU287
GILE41-GLY61
GLYS107-TRP127
GLEU218-SER238
GLEU267-LEU287
ALEU218-SER238
ALEU267-LEU287
BILE41-GLY61
BLYS107-TRP127
BLEU218-SER238
BLEU267-LEU287
CILE41-GLY61

site_idSWS_FT_FI3
Number of Residues497
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ATHR62-HIS106
ESER239-LYS266
FTHR62-HIS106
FSER239-LYS266
GTHR62-HIS106
GSER239-LYS266
ASER239-LYS266
BTHR62-HIS106
BSER239-LYS266
CTHR62-HIS106
CSER239-LYS266
DTHR62-HIS106
DSER239-LYS266
ETHR62-HIS106

site_idSWS_FT_FI4
Number of Residues14
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q9JIP4
ChainResidueDetails
ACYS40
ECYS347
FCYS40
FCYS347
GCYS40
GCYS347
ACYS347
BCYS40
BCYS347
CCYS40
CCYS347
DCYS40
DCYS347
ECYS40

site_idSWS_FT_FI5
Number of Residues7
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:30814251
ChainResidueDetails
ATYR199
BTYR199
CTYR199
DTYR199
ETYR199
FTYR199
GTYR199

site_idSWS_FT_FI6
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17715132, ECO:0000269|PubMed:30918116, ECO:0000269|PubMed:32494015, ECO:0000269|PubMed:33947837
ChainResidueDetails
AALA255
BALA255
CALA255
DALA255
EALA255
FALA255
GALA255

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PDB entries from 2024-07-17

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