Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5CUR

G158E/K44E/R57E/Y49E Bacillus subtilis lipase A with 20% [BMIM][Cl]

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005576cellular_componentextracellular region
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue BM0 A 201
ChainResidue
ATYR37
APHE58
ALYS61
AGLU65
AGLN121
AHOH392

site_idAC2
Number of Residues6
Detailsbinding site for residue BM0 A 202
ChainResidue
ABM0203
AHOH419
AHOH532
AALA20
AGLY21
ATYR161

site_idAC3
Number of Residues3
Detailsbinding site for residue BM0 A 203
ChainResidue
APHE17
ATYR139
ABM0202

site_idAC4
Number of Residues11
Detailsbinding site for residue BM0 A 204
ChainResidue
AILE12
AGLY13
AASN18
AHIS76
ASER77
AHIS156
AILE157
ALEU160
ACL207
AHOH388
AHOH516

site_idAC5
Number of Residues7
Detailsbinding site for residue BM0 A 205
ChainResidue
AHIS3
AGLN29
AGLY30
ATRP31
ALEU173
AASN174
AHOH311

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 206
ChainResidue
AMET134
AHIS156

site_idAC7
Number of Residues5
Detailsbinding site for residue CL A 207
ChainResidue
AHIS10
AGLY11
AASN18
AHIS76
ABM0204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
ASER77

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
AASP133
AHIS156

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 518
ChainResidueDetails
AILE12electrostatic stabiliser
ASER77covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AMET78electrostatic stabiliser
AASP133electrostatic stabiliser, increase basicity, modifies pKa
AHIS156proton acceptor, proton donor

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon