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4H0S

Crystal structure analysis of a basic phospholipase A2 from Trimeresurus stejnegeri venom

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0050482biological_processarachidonic acid secretion
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0050482biological_processarachidonic acid secretion
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0050482biological_processarachidonic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 201
ChainResidue
ATRP77
AHOH315
BHOH378

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 202
ChainResidue
AGLU17
BASN79

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 201
ChainResidue
BLYS7
BTYR75
BTRP77
BHOH331

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 202
ChainResidue
BGLU17
BILE19
BLEU20

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA C 201
ChainResidue
CGLN4
CLYS7

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCECDKAVaTC
ChainResidueDetails
AVAL95-CYS105

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. SCSTkwDsYSYSWEN
ChainResidueDetails
ASER59-ASN79

221716

PDB entries from 2024-06-26

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