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3T8B

Crystal structure of Mycobacterium tuberculosis MenB with altered hexameric assembly

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008935molecular_function1,4-dihydroxy-2-naphthoyl-CoA synthase activity
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0034214biological_processprotein hexamerization
B0005886cellular_componentplasma membrane
B0008935molecular_function1,4-dihydroxy-2-naphthoyl-CoA synthase activity
B0009234biological_processmenaquinone biosynthetic process
B0016829molecular_functionlyase activity
B0034214biological_processprotein hexamerization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 315
ChainResidue
AGLY83
APRO147
ALYS148
AVAL149
APRO255
AARG259
AHOH333
AHOH387

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16131752","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12909628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20643650","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21830810","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 346
ChainResidueDetails
AGLY105electrostatic stabiliser, hydrogen bond donor
AGLY161electrostatic stabiliser, hydrogen bond donor
AASP185activator
ASER190activator

site_idMCSA2
Number of Residues3
DetailsM-CSA 346
ChainResidueDetails
BGLY105electrostatic stabiliser, hydrogen bond donor
BGLY161electrostatic stabiliser, hydrogen bond donor
BASP185activator

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PDB entries from 2025-12-24

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