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6AJG

Crystal structure of mycolic acid transporter MmpL3 from Mycobacterium smegmatis complexed with SQ109

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 3RX A 1001
ChainResidue
AILE249
AASP645
AILE253
AASP256
ATYR257
AILE297
ASER301
AALA637
AVAL638
ALEU642

site_idAC2
Number of Residues11
Detailsbinding site for residue LMT A 1002
ChainResidue
ATHR66
ASER67
AVAL109
AASP119
ATHR121
ASER136
ALEU171
ALEU174
AGLN442
AARG453
ALMT1003

site_idAC3
Number of Residues14
Detailsbinding site for residue LMT A 1003
ChainResidue
AGLN40
AASP64
ASER67
AILE182
AHIS239
APHE240
APHE241
AILE427
AARG453
ATHR454
AGLU455
ATHR549
ALEU698
ALMT1002

site_idAC4
Number of Residues7
Detailsbinding site for residue LMT A 1004
ChainResidue
ALEU422
ASER423
ALEU424
AGLN554
AILE557
ALEU564
ALEU600

site_idAC5
Number of Residues7
Detailsbinding site for residue LMT A 1005
ChainResidue
ALEU23
AGLY27
ATYR30
AASP77
ALYS79
AGLU234
APHE235

site_idAC6
Number of Residues10
Detailsbinding site for residue LMT A 1006
ChainResidue
ALEU25
AILE32
AGLY35
ATHR179
AGLY180
AILE182
AGLY183
ALEU226
APHE240
AGLN243

site_idAC7
Number of Residues9
Detailsbinding site for residue LMT A 1007
ChainResidue
AGLN-3
ATHR285
AARG288
ATHR289
APHE292
ALEU581
AALA582
ASER652
AARG653

site_idAC8
Number of Residues7
Detailsbinding site for residue LMT A 1008
ChainResidue
ATRP390
ATHR672
AALA673
AGLY676
ATHR680
AARG720
AMET721

site_idAC9
Number of Residues4
Detailsbinding site for residue LMT A 1009
ChainResidue
ATHR236
ALYS313
ATYR317
ALMT1010

site_idAD1
Number of Residues2
Detailsbinding site for residue LMT A 1010
ChainResidue
ATYR317
ALMT1009

site_idAD2
Number of Residues8
Detailsbinding site for residue MHA A 1011
ChainResidue
AASP759
ATHR891
APRO892
AASN893
AARG894
AILE917
ALYS918
AALA919

site_idAD3
Number of Residues7
Detailsbinding site for residue MHA A 1012
ChainResidue
AGLY618
AGLY862
APHE863
ATHR864
AASN865
ASER866
AASN881

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues131
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875
ChainResidueDetails
AMET1-TYR14
AVAL262-VAL290
AALA339-PRO401
APRO589-LYS591
ASER652-LEU678

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AILE15-GLY35
AMET631-VAL651
AILE679-VAL699
ALEU704-VAL724
AVAL197-ILE217
AGLY218-VAL238
APHE241-ILE261
AVAL291-PHE311
AALA318-LEU338
AILE402-LEU422
AALA568-LEU588
AALA592-VAL612

site_idSWS_FT_FI3
Number of Residues330
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875
ChainResidueDetails
AASN36-LEU196
AHIS239-PHE240
ALEU312-TYR317
ASER423-MET567
AASP613-PRO630
AMET700-TYR703

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31113875, ECO:0007744|PDB:6OR2
ChainResidueDetails
AGLN40

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30682372, ECO:0007744|PDB:6AJG
ChainResidueDetails
AASP645

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Part of the proton-transportation channel => ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875
ChainResidueDetails
AASP256
ATYR257
ATYR646

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Part of the proton transportation network => ECO:0000305|PubMed:31113875
ChainResidueDetails
ALYS591
AGLU647

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Part of the proton-transportation channel => ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875, ECO:0000305|PubMed:32512002
ChainResidueDetails
AASP645

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PDB entries from 2025-07-02

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