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

5CRI

Wild-type Bacillus subtilis lipase A with 0% [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
B0004806molecular_functiontriglyceride lipase activity
B0005576cellular_componentextracellular region
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 201
ChainResidue
AVAL154
ASER162
ASER163
AGLN164

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 202
ChainResidue
AHOH446
BARG33
BMET137
BTYR139
AARG142
AHOH304
AHOH355
AHOH398
AHOH441

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 203
ChainResidue
ALYS122
AGLY155
AHIS156
AILE157
AGLY158
AASN181
AHOH330
AHOH351

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 204
ChainResidue
AASN50
AHOH314
AHOH323
AHOH449
BSER162
BSER163
BHOH331

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 B 201
ChainResidue
BTYR129
BARG142
BGLN150
BHOH305
BHOH327
BHOH383
BHOH393
BHOH411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
ASER77
BSER77

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
AASP133
AHIS156
BASP133
BHIS156

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

site_idMCSA2
Number of Residues5
DetailsM-CSA 518
ChainResidueDetails
BILE12electrostatic stabiliser
BSER77covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BMET78electrostatic stabiliser
BASP133electrostatic stabiliser, increase basicity, modifies pKa
BHIS156proton acceptor, proton donor

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon