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1VL9

Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0002227biological_processinnate immune response in mucosa
A0004623molecular_functionphospholipase A2 activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006644biological_processphospholipid metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0009986cellular_componentcell surface
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0032052molecular_functionbile acid binding
A0046470biological_processphosphatidylcholine metabolic process
A0046471biological_processphosphatidylglycerol metabolic process
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0048146biological_processpositive regulation of fibroblast proliferation
A0050482biological_processarachidonic acid secretion
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A1904635biological_processpositive regulation of podocyte apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 124
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH204
AHOH206

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 125
ChainResidue
AHOH207
AHOH212
AHOH431
AASN71
AASN72
AGLU92

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 126
ChainResidue
ALYS12
AGLU81
AILE82
AARG100
AILE104
AHOH264

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD A 1603
ChainResidue
AMET56
ATYR69
AHOH387
AHOH399
AMPD1602
AMPD1605

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MRD A 1604
ChainResidue
ALEU2
APRO18
APHE22
AGLY30
AHOH206

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MRD A 1606
ChainResidue
ASER15
ATYR111
AHOH438

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MPD A 1601
ChainResidue
AASN23
AASN24
AGLY26
ACYS27
ACYS29
AGLY30
ALEU31
AGLY32
ALEU118
AHOH210
AHOH227
AHOH305
AHOH370
AHOH376
AHOH380
AHOH385

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 1602
ChainResidue
ALEU31
AASP49
AMET56
ATYR69
AHOH204
AMRD1603

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 1605
ChainResidue
ALEU2
ALEU58
APHE94
AHOH313
AHOH387
AMRD1603

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQtHDnC
ChainResidueDetails
ACYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:7464926
ChainResidueDetails
AHIS48
AASP99

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

221051

PDB entries from 2024-06-12

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