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6VKS

Cryo-electron microscopy structures of a gonococcal multidrug efflux pump illuminate a mechanism of drug recognition with ampicillin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0009636biological_processresponse to toxic substance
A0015562molecular_functionefflux transmembrane transporter activity
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0055085biological_processtransmembrane transport
B0005886cellular_componentplasma membrane
B0009636biological_processresponse to toxic substance
B0015562molecular_functionefflux transmembrane transporter activity
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0042908biological_processxenobiotic transport
B0042910molecular_functionxenobiotic transmembrane transporter activity
B0055085biological_processtransmembrane transport
C0005886cellular_componentplasma membrane
C0009636biological_processresponse to toxic substance
C0015562molecular_functionefflux transmembrane transporter activity
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0042908biological_processxenobiotic transport
C0042910molecular_functionxenobiotic transmembrane transporter activity
C0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PTY A 1101
ChainResidue
AARG8
APHE18
BILE441
BLEU888
BPTY1101

site_idAC2
Number of Residues3
Detailsbinding site for residue PTY A 1102
ChainResidue
ATRP13
AILE17
BPTY1103

site_idAC3
Number of Residues4
Detailsbinding site for residue PTY A 1103
ChainResidue
APHE1040
ATHR1043
CPTY1104
ATRP892

site_idAC4
Number of Residues5
Detailsbinding site for residue PTY B 1101
ChainResidue
APTY1101
BMET1
BPHE5
BSER437
BPTY1102

site_idAC5
Number of Residues4
Detailsbinding site for residue PTY B 1102
ChainResidue
BPHE11
BPTY1101
CALA887
CLEU888

site_idAC6
Number of Residues6
Detailsbinding site for residue PTY B 1103
ChainResidue
APTY1102
BPHE882
BTRP892
BLEU896
BLEU899
BPHE1040

site_idAC7
Number of Residues8
Detailsbinding site for residue PTY B 1104
ChainResidue
BALA21
BALA22
BILE24
BPHE25
CMET456
CALA872
CALA875
CPTY1103

site_idAC8
Number of Residues5
Detailsbinding site for residue PTY B 1105
ChainResidue
BILE27
BASN296
BILE335
BLEU374
BPHE378

site_idAC9
Number of Residues4
Detailsbinding site for residue AIX B 1106
ChainResidue
BPHE136
BPHE176
BVAL607
BPHE610

site_idAD1
Number of Residues8
Detailsbinding site for residue PTY C 1101
ChainResidue
AGLY438
ALEU888
AMET1049
CPHE4
CARG8
CPHE11
CPHE18
CPTY1102

site_idAD2
Number of Residues5
Detailsbinding site for residue PTY C 1102
ChainResidue
CLYS3
CPHE4
CPTY1101
CPTY1107
CPTY1108

site_idAD3
Number of Residues3
Detailsbinding site for residue PTY C 1104
ChainResidue
APTY1103
CILE17
CPTY1105

site_idAD4
Number of Residues4
Detailsbinding site for residue PTY C 1105
ChainResidue
CTRP13
CARG361
CMET494
CPTY1104

site_idAD5
Number of Residues3
Detailsbinding site for residue PTY C 1106
ChainResidue
CILE27
CILE343
CPTY1109

site_idAD6
Number of Residues6
Detailsbinding site for residue PTY C 1107
ChainResidue
CMET1
CPHE4
CPHE5
CPHE481
CPTY1102
CPTY1108

site_idAD7
Number of Residues2
Detailsbinding site for residue PTY C 1108
ChainResidue
CPTY1102
CPTY1107

site_idAD8
Number of Residues4
Detailsbinding site for residue PTY C 1109
ChainResidue
CILE339
CLEU374
CMET393
CPTY1106

site_idAD9
Number of Residues13
Detailsbinding site for Di-peptide PTY C 1103 and PHE C 1040
ChainResidue
BPTY1104
CVAL879
CPHE882
CSER891
CTRP892
CSER893
CLEU896
CVAL1036
CARG1037
CLYS1038
CPHE1039
CLYS1041
CGLU1042

240971

PDB entries from 2025-08-27

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