Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BD1

A possible role of the second calcium ion in interfacial binding: Atomic and medium resolution crystal structures of the quadruple mutant of 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_processarachidonate secretion
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A1904635biological_processpositive regulation of podocyte apoptotic process
B0002227biological_processinnate immune response in mucosa
B0004623molecular_functionphospholipase A2 activity
B0005102molecular_functionsignaling receptor binding
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006644biological_processphospholipid metabolic process
B0008284biological_processpositive regulation of cell population proliferation
B0009986cellular_componentcell surface
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0019731biological_processantibacterial humoral response
B0032052molecular_functionbile acid binding
B0046470biological_processphosphatidylcholine metabolic process
B0046471biological_processphosphatidylglycerol metabolic process
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0048146biological_processpositive regulation of fibroblast proliferation
B0050482biological_processarachidonate secretion
B0050830biological_processdefense response to Gram-positive bacterium
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B1904635biological_processpositive regulation of podocyte apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 847
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH202
AHOH208

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 848
ChainResidue
AHOH226
AHOH238
AHOH239
AASN71
AASN72
AGLU92

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 849
ChainResidue
BTYR28
BGLY30
BGLY32
BASP49
BHOH203
BHOH206

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 850
ChainResidue
BASN71
BASN72
BGLU92
BHOH245
BHOH254
BHOH261

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 723
ChainResidue
APHE22
AGLY30
ALEU31
AHIS48
AHOH202

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 724
ChainResidue
BPHE22
BGLY30
BHOH203

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 Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:7464926
ChainResidueDetails
AHIS48
AASP99
BHIS48
BASP99

site_idSWS_FT_FI2
Number of Residues8
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
BTYR28
BGLY30
BGLY32
BASP49

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP99

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon