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1HPL

HORSE PANCREATIC LIPASE. THE CRYSTAL STRUCTURE AT 2.3 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0042572biological_processretinol metabolic process
A0046872molecular_functionmetal ion binding
A0047376molecular_functionall-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0004806molecular_functiontriglyceride lipase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
B0042572biological_processretinol metabolic process
B0046872molecular_functionmetal ion binding
B0047376molecular_functionall-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 960
ChainResidue
AASP195
AHOH1074
AHOH1261
AGLU187
AARG190
AASP192

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 970
ChainResidue
BGLU187
BARG190
BASP192
BASP195
BHOH1079
BHOH1162

site_idACT
Number of Residues3
DetailsACTIVE SITE IN CHAIN A
ChainResidue
ASER152
AASP176
AHIS263

site_idBCT
Number of Residues3
DetailsACTIVE SITE IN CHAIN B
ChainResidue
BSER152
BASP176
BHIS263

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VHIIGHSLGS
ChainResidueDetails
AVAL146-SER155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER152
BSER152

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AASP176
AHIS263
BASP176
BHIS263

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU187
AARG190
AASP192
AASP195
BGLU187
BARG190
BASP192
BASP195

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 8182745, 9109604
ChainResidueDetails
AHIS263
APHE77
AASP176
ALEU153

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 8182745, 9109604
ChainResidueDetails
BHIS263
BPHE77
BASP176
BLEU153

site_idMCSA1
Number of Residues5
DetailsM-CSA 218
ChainResidueDetails
APHE77electrostatic stabiliser, hydrogen bond donor
ASER152covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ALEU153electrostatic stabiliser, hydrogen bond donor
AASP176activator, hydrogen bond acceptor
AHIS263hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 218
ChainResidueDetails
BPHE77electrostatic stabiliser, hydrogen bond donor
BSER152covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BLEU153electrostatic stabiliser, hydrogen bond donor
BASP176activator, hydrogen bond acceptor
BHIS263hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-09-11

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