Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1XXW

Structure of zinc induced heterodimer of two calcium free isoforms of phospholipase A2 from Naja naja sagittifera at 2.7A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AASP24
AASN112
AHOH303
AHOH350
BASP24

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 301
ChainResidue
AHOH391

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 302
ChainResidue
BARG31
AHIS48
AASP49
ALYS64

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQvHDnC
ChainResidueDetails
BCYS44-CYS51
ACYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC
ChainResidueDetails
BVAL90-CYS100
AVAL90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
BHIS48
BASP94

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15828003, ECO:0007744|PDB:1S6B
ChainResidueDetails
BTYR28
BGLY30
BGLY32
BASP49

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP94

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP94

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon