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7C2N

Crystal structure of mycolic acid transporter MmpL3 from Mycobacterium smegmatis complexed with SPIRO

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue L6T A 1001
ChainResidue
AGLU46
APHE240
ASER54
ALEU55
AASP58
AARG63
AASP64
AASP144
ALEU171
AHIS239

site_idAC2
Number of Residues5
Detailsbinding site for residue L6T A 1002
ChainResidue
AVAL109
ATHR121
AVAL122
AMET125
AARG453

site_idAC3
Number of Residues9
Detailsbinding site for residue L6T A 1003
ChainResidue
AGLN-3
AARG288
AVAL291
APHE292
ALEU581
ASER652
AARG653
AGLU656
AARG744

site_idAC4
Number of Residues7
Detailsbinding site for residue L6T A 1004
ChainResidue
ATRP609
AHIS615
AGLY618
ALEU619
ALEU713
ALYS884
AMHA1007

site_idAC5
Number of Residues4
Detailsbinding site for residue L6T A 1005
ChainResidue
AARG188
AALA192
AASN621
AALA692

site_idAC6
Number of Residues7
Detailsbinding site for residue MHA A 1006
ChainResidue
AASP759
ATHR891
AASN893
AARG894
AILE917
ALYS918
AALA919

site_idAC7
Number of Residues7
Detailsbinding site for residue MHA A 1007
ChainResidue
AGLY862
APHE863
ATHR864
AASN865
ASER866
AASN881
AL6T1004

site_idAC8
Number of Residues11
Detailsbinding site for residue FG0 A 1008
ChainResidue
AILE249
AILE253
APHE260
ASER293
AILE297
AVAL638
AGLY641
ALEU642
AASP645
ATYR646
APHE649

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues69
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues330
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues28
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues19
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OR2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AJG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsSite: {"description":"Part of the proton-transportation channel","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Part of the proton transportation network","evidences":[{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsSite: {"description":"Part of the proton-transportation channel","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32512002","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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