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8WIW

Cryo-EM structure of the flagellar C ring in the CW state

This is a non-PDB format compatible entry.
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9
ChainResidueDetails
hASP12
ANASP12
ATASP12
AZASP12
AfASP12
AlASP12
ArASP12
AxASP12
A5ASP12
BBASP12
BIASP12
iASP12
BPASP12
BWASP12
BdASP12
BkASP12
BrASP12
ByASP12
B6ASP12
CCASP12
CJASP12
CQASP12
jASP12
CXASP12
CeASP12
ClASP12
CsASP12
CzASP12
A9ILE26-ALA46
A9PHE455-LEU475
BFILE26-ALA46
BFPHE455-LEU475
BMILE26-ALA46
kASP12
BMPHE455-LEU475
BTILE26-ALA46
BTPHE455-LEU475
BaILE26-ALA46
BaPHE455-LEU475
BhILE26-ALA46
BhPHE455-LEU475
BoILE26-ALA46
BoPHE455-LEU475
BvILE26-ALA46
lASP12
BvPHE455-LEU475
B3ILE26-ALA46
B3PHE455-LEU475
B0ILE26-ALA46
B0PHE455-LEU475
CGILE26-ALA46
CGPHE455-LEU475
CNILE26-ALA46
CNPHE455-LEU475
CUILE26-ALA46
mASP12
CUPHE455-LEU475
CbILE26-ALA46
CbPHE455-LEU475
CiILE26-ALA46
CiPHE455-LEU475
CpILE26-ALA46
CpPHE455-LEU475
CwILE26-ALA46
CwPHE455-LEU475
nASP12
4ASP12
9ASP12

site_idSWS_FT_FI2
Number of Residues102
DetailsBINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC
ChainResidueDetails
hLYS13
kLYS13
CzLYS13
CzASP57
CzASN59
kASP57
kASN59
lLYS13
lASP57
lASN59
mLYS13
mASP57
mASN59
nLYS13
hASP57
nASP57
nASN59
4LYS13
4ASP57
4ASN59
9LYS13
9ASP57
9ASN59
ANLYS13
ANASP57
hASN59
ANASN59
ATLYS13
ATASP57
ATASN59
AZLYS13
AZASP57
AZASN59
AfLYS13
AfASP57
AfASN59
iLYS13
AlLYS13
AlASP57
AlASN59
ArLYS13
ArASP57
ArASN59
AxLYS13
AxASP57
AxASN59
A5LYS13
iASP57
A5ASP57
A5ASN59
BBLYS13
BBASP57
BBASN59
BILYS13
BIASP57
BIASN59
BPLYS13
BPASP57
iASN59
BPASN59
BWLYS13
BWASP57
BWASN59
BdLYS13
BdASP57
BdASN59
BkLYS13
BkASP57
BkASN59
jLYS13
BrLYS13
BrASP57
BrASN59
ByLYS13
ByASP57
ByASN59
B6LYS13
B6ASP57
B6ASN59
CCLYS13
jASP57
CCASP57
CCASN59
CJLYS13
CJASP57
CJASN59
CQLYS13
CQASP57
CQASN59
CXLYS13
CXASP57
jASN59
CXASN59
CeLYS13
CeASP57
CeASN59
ClLYS13
ClASP57
ClASN59
CsLYS13
CsASP57
CsASN59

site_idSWS_FT_FI3
Number of Residues34
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143
ChainResidueDetails
hASP57
ANASP57
ATASP57
AZASP57
AfASP57
AlASP57
ArASP57
AxASP57
A5ASP57
BBASP57
BIASP57
iASP57
BPASP57
BWASP57
BdASP57
BkASP57
BrASP57
ByASP57
B6ASP57
CCASP57
CJASP57
CQASP57
jASP57
CXASP57
CeASP57
ClASP57
CsASP57
CzASP57
kASP57
lASP57
mASP57
nASP57
4ASP57
9ASP57

site_idSWS_FT_FI4
Number of Residues68
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
hLYS92
lLYS109
mLYS92
mLYS109
nLYS92
nLYS109
4LYS92
4LYS109
9LYS92
9LYS109
ANLYS92
hLYS109
ANLYS109
ATLYS92
ATLYS109
AZLYS92
AZLYS109
AfLYS92
AfLYS109
AlLYS92
AlLYS109
ArLYS92
iLYS92
ArLYS109
AxLYS92
AxLYS109
A5LYS92
A5LYS109
BBLYS92
BBLYS109
BILYS92
BILYS109
BPLYS92
iLYS109
BPLYS109
BWLYS92
BWLYS109
BdLYS92
BdLYS109
BkLYS92
BkLYS109
BrLYS92
BrLYS109
ByLYS92
jLYS92
ByLYS109
B6LYS92
B6LYS109
CCLYS92
CCLYS109
CJLYS92
CJLYS109
CQLYS92
CQLYS109
CXLYS92
jLYS109
CXLYS109
CeLYS92
CeLYS109
ClLYS92
ClLYS109
CsLYS92
CsLYS109
CzLYS92
CzLYS109
kLYS92
kLYS109
lLYS92

224572

PDB entries from 2024-09-04

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