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5CT6

Wild-type 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
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 Residues5
Detailsbinding site for residue CL A 201
ChainResidue
AGLY155
AHIS156
AILE157
AGLY158
BGLY155

site_idAC2
Number of Residues7
Detailsbinding site for residue BM0 A 202
ChainResidue
ASER77
AHIS156
AHOH305
AILE12
AGLY13
AGLY14
AASN18

site_idAC3
Number of Residues9
Detailsbinding site for residue BM0 A 203
ChainResidue
ATYR49
AASN50
AHOH302
BHIS3
BLYS35
BTHR66
BGLY67
BALA68
BMET137

site_idAC4
Number of Residues4
Detailsbinding site for residue BM0 A 204
ChainResidue
ATHR45
ATHR47
AHOH396
BLEU108

site_idAC5
Number of Residues6
Detailsbinding site for residue BM0 A 205
ChainResidue
AGLY116
AASP118
APRO119
ALYS122
AHOH375
BHOH348

site_idAC6
Number of Residues6
Detailsbinding site for residue BM0 A 206
ChainResidue
AASP34
ALEU36
ATYR37
AARG107
AARG142
AASP144

site_idAC7
Number of Residues4
Detailsbinding site for residue CL B 201
ChainResidue
AGLY155
AHOH306
BHIS156
BILE157

site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 202
ChainResidue
BTHR47
BASN48
BHOH380

site_idAC9
Number of Residues5
Detailsbinding site for residue BM0 B 203
ChainResidue
AILE157
BTRP42
BGLY158
BTYR161
BHOH367

site_idAD1
Number of Residues7
Detailsbinding site for residue BM0 B 204
ChainResidue
BASP34
BLEU36
BTYR37
BARG107
BARG142
BASP144
BHOH381

site_idAD2
Number of Residues3
Detailsbinding site for residue BM0 B 205
ChainResidue
ATYR161
BPHE17
BTYR161

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

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PDB entries from 2024-08-07

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