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6EIC

Crystal structure of Rv0183, a Monoglyceride Lipase from Mycobacterium Tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004622molecular_functionphosphatidylcholine lysophospholipase activity
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0046503biological_processglycerolipid catabolic process
A0047372molecular_functionmonoacylglycerol lipase activity
A0052151biological_processsymbiont-mediated activation of host apoptosis
B0004622molecular_functionphosphatidylcholine lysophospholipase activity
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
B0046503biological_processglycerolipid catabolic process
B0047372molecular_functionmonoacylglycerol lipase activity
B0052151biological_processsymbiont-mediated activation of host apoptosis
C0004622molecular_functionphosphatidylcholine lysophospholipase activity
C0005576cellular_componentextracellular region
C0005886cellular_componentplasma membrane
C0006629biological_processlipid metabolic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0016020cellular_componentmembrane
C0016042biological_processlipid catabolic process
C0016298molecular_functionlipase activity
C0016787molecular_functionhydrolase activity
C0046503biological_processglycerolipid catabolic process
C0047372molecular_functionmonoacylglycerol lipase activity
C0052151biological_processsymbiont-mediated activation of host apoptosis
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 C 301
ChainResidue
CLEU39
CLEU166
CHOH422

site_idAC2
Number of Residues6
Detailsbinding site for residue MPD C 302
ChainResidue
CLEU39
CGLU41
CHIS109
CSER110
CHIS256
CGLU257

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD A 301
ChainResidue
ALEU39
AHIS109
ASER110
ATYR181
ALEU228
AHIS256
AGLU257

site_idAC4
Number of Residues7
Detailsbinding site for residue MPD B 301
ChainResidue
BGLY38
BLEU39
BARG45
BHIS109
BTYR181
BHIS256
BGLU257

site_idAC5
Number of Residues3
Detailsbinding site for residue NO3 B 302
ChainResidue
BLEU39
BLEU200
BHOH428

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:17784850, ECO:0000305|PubMed:29895832
ChainResidueDetails
CSER110
ASER110
BSER110

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:17784850, ECO:0000305|PubMed:29895832
ChainResidueDetails
CASP226
CHIS256
AASP226
AHIS256
BASP226
BHIS256

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PDB entries from 2025-06-18

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