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

3V9M

Phospholipase ACII4 from Australian King Brown Snake

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonate secretion
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonate secretion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 201
ChainResidue
APHE5
AHOH403
AHOH433
AHOH440

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AHOH430
APRO82
ACYS84
ALYS85
AHOH408
AHOH417

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AGLN4
AASN7
ATRP69
AHOH400
AHOH401
AHOH402
BGLN4
BASN7
BTRP69

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
ASER16
AARG17
ATYR104
ALYS115

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 205
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH440
AHOH468

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 206
ChainResidue
ATRP31
ALYS63
AHOH403
BCYS60

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
BPRO82
BGLY83
BCYS84
BLYS85
BHOH356
BHOH458

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BTYR28
BGLY30
BGLY32
BASP49
BHOH459
BHOH460

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 203
ChainResidue
BTYR22
BHOH371
BHOH460

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 204
ChainResidue
AGLY56
ACYS60
BTRP31
BLYS63
BHOH402

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCACDAAAaKC
ChainResidueDetails
AVAL88-CYS98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS48
AASP92
BHIS48
BASP92

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0007744|PDB:3V9M
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49
BTYR28
BGLY30
BGLY32
BASP49

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon