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4LIP

PSEUDOMONAS LIPASE COMPLEXED WITH RC-(RP, SP)-DIBUTYLCARBAMOYLGLYCERO-3-O-BUTYLPHOSPHONATE

Functional Information from GO Data
ChainGOidnamespacecontents
D0004806molecular_functiontriglyceride lipase activity
D0005576cellular_componentextracellular region
D0016042biological_processlipid catabolic process
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0004806molecular_functiontriglyceride lipase activity
E0005576cellular_componentextracellular region
E0016042biological_processlipid catabolic process
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA D 321
ChainResidue
DASP242
DASP288
DGLN292
DLEU293
DVAL296
DHOH975
DHOH988

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA E 321
ChainResidue
EASP242
EASP288
EGLN292
ELEU293
EVAL296
EHOH985
EHOH998

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CCP D 950
ChainResidue
DGLY16
DLEU17
DSER87
DGLN88
DSER117
DVAL267
DHIS286

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CCP E 950
ChainResidue
EGLY16
ELEU17
ESER87
EGLN88
ESER117
ELEU167
EVAL267
EHIS286

site_idACD
Number of Residues3
DetailsACTIVE SITE
ChainResidue
DSER87
DHIS286
DASP264

site_idACE
Number of Residues3
DetailsACTIVE SITE
ChainResidue
ESER87
EHIS286
EASP264

site_idOXD
Number of Residues2
DetailsOXYANION HOLE
ChainResidue
DLEU17
DGLN88

site_idOXE
Number of Residues2
DetailsOXYANION HOLE
ChainResidue
EGLN88
ELEU17

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VNLVGHSQGG
ChainResidueDetails
DVAL81-GLY90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:15850979, ECO:0000305|PubMed:18386861, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP
ChainResidueDetails
DSER87
ESER87

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP
ChainResidueDetails
DASP264
DHIS286
EASP264
EHIS286

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP
ChainResidueDetails
DLEU17
DGLN88
ELEU17
EGLN88

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP
ChainResidueDetails
DASP242
DASP288
DGLN292
DVAL296
EASP242
EASP288
EGLN292
EVAL296

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
DASP264
DHIS286
DSER87

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
EASP264
EHIS286
ESER87

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
DASP264
DHIS286
DLEU17
DGLN88
DSER87

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
EASP264
EHIS286
ELEU17
EGLN88
ESER87

221716

PDB entries from 2024-06-26

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