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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_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
AVAL197-ILE217
AGLY218-VAL238
APHE241-ILE261
AVAL291-PHE311
AALA318-LEU338
AILE402-LEU422
AALA568-LEU588
AALA592-VAL612
AMET631-VAL651
AILE679-VAL699
ALEU704-VAL724

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
ATYR646
AASP256
ATYR257

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

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 2024-06-12

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