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2ES4

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0004806molecular_functiontriglyceride lipase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
D0006457biological_processprotein folding
D0016020cellular_componentmembrane
D0051082molecular_functionunfolded protein binding
E0006457biological_processprotein folding
E0016020cellular_componentmembrane
E0051082molecular_functionunfolded protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 999
ChainResidue
AASP241
AASP287
AGLN291
ALEU292
AVAL295
AHOH1056
AHOH1064

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 998
ChainResidue
BGLN291
BLEU292
BVAL295
BHOH1066
BHOH1087
BASP241
BASP287

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD B 903
ChainResidue
BGLN34
BVAL46
BHOH1075
EGLN234

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD B 904
ChainResidue
BGLU197
BHOH1266
EGLN256

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 906
ChainResidue
BGLY188

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 907
ChainResidue
BGLN261

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VNLIGHSQGG
ChainResidueDetails
AVAL81-GLY90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:8683577
ChainResidueDetails
AASN48
BASN48

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:8683577
ChainResidueDetails
ATHR224
AALA246
BTHR224
BALA246

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22088
ChainResidueDetails
ALEU49
BLEU49
ALEU17
AGLN88
BLEU17
BGLN88

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8683577, ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE
ChainResidueDetails
ASER202
ALEU248
AALA252
AASN256
BSER202
BLEU248
BALA252
BASN256

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:1476423, ECO:0000305|PubMed:8405390
ChainResidueDetails
ASER87
BSER87

site_idSWS_FT_FI6
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:1476423, ECO:0000305|PubMed:8405390
ChainResidueDetails
AASP263
AHIS285
BASP263
BHIS285

site_idSWS_FT_FI7
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH, ECO:0007744|PDB:2ES4
ChainResidueDetails
AASP241
AASP287
AGLN291
AVAL295
BASP241
BASP287
BGLN291
BVAL295

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
AHIS285
ASER87
AASP263

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
BHIS285
BSER87
BASP263

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
ALEU17
AHIS285
AGLN88
ASER87
AASP263

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
BLEU17
BHIS285
BGLN88
BSER87
BASP263

site_idMCSA1
Number of Residues9
DetailsM-CSA 519
ChainResidueDetails
ALEU17electrostatic stabiliser
ASER87covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AGLN88electrostatic stabiliser
AASP241metal ligand
AASP263electrostatic stabiliser, increase basicity, modifies pKa
AHIS285proton acceptor, proton donor
AASP287metal ligand
AGLN291metal ligand
AVAL295metal ligand

site_idMCSA2
Number of Residues9
DetailsM-CSA 519
ChainResidueDetails
BLEU17electrostatic stabiliser
BSER87covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BGLN88electrostatic stabiliser
BASP241metal ligand
BASP263electrostatic stabiliser, increase basicity, modifies pKa
BHIS285proton acceptor, proton donor
BASP287metal ligand
BGLN291metal ligand
BVAL295metal ligand

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PDB entries from 2024-07-24

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