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4E4C

Crystal structure of Notexin at 1.8 A 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
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AASN80
AHOH367
AILE81
ALYS82
ALYS83
ATRP110
AASN111
AHOH308
AHOH326
AHOH333

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AARG17
AARG17
APRO104
ATYR105
AASN107
AHOH310
AHOH310
AHOH321
AHOH325

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 203
ChainResidue
ASER6
APRO18
ATHR19
ATRP20
APHE61
AHOH356

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDVEAaFC
ChainResidueDetails
AVAL89-CYS99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:1245225
ChainResidueDetails
AHIS48
AASP93

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P60043
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

224931

PDB entries from 2024-09-11

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