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2BAX

Atomic Resolution Structure of the Double Mutant (K53,56M) 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_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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 124
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH257
AHOH262

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 125
ChainResidue
AILE104
AHOH263
ALYS12
AGLU81
AILE82

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MRD A 127
ChainResidue
APHE5
AILE9
APRO18
ALEU19
APHE22
AASN23
AGLY30
AHIS48
ATYR69
AHOH257
AHOH393

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MRD A 130
ChainResidue
APHE22
ASER107
ALYS108
AVAL109
APRO110
AMRD131
AHOH240
AHOH248
AHOH271
AHOH289
AHOH312
AHOH366

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MRD A 131
ChainResidue
AILE13
ASER15
ASER16
AASP21
AASN97
ATYR111
AMRD130
AHOH218
AHOH235
AHOH264
AHOH282

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE MRD A 132
ChainResidue
AASN24
ATYR25
AGLY26
ACYS27
ATYR28
ACYS29
AGLY30
ALEU31
AGLY32
AGLY33
AVAL65
ALYS120
AHOH314
AHOH322
AHOH408

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MPD A 128
ChainResidue
AASN6
AGLU17
ALEU19
ALEU20
AILE104
ACYS105
ALYS108
AVAL109
AHOH202
AHOH230
AHOH293
AHOH353
AHOH364

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

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

234136

PDB entries from 2025-04-02

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