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1YXH

Crystal structure of a novel phospholipase A2 from Naja naja sagittifera with a strong anticoagulant activity

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AEOH2002
AHOH3050

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 3001
ChainResidue
ASER34
AGLN120

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH A 2001
ChainResidue
AEOH2002
APHE22

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EOH A 2002
ChainResidue
ATYR28
AGLY30
AASP49
ACA1001
AEOH2001
AHOH3052

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. VCDCDRLAaIC
ChainResidueDetails
AVAL90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:16269164
ChainResidueDetails
AHIS48
AASP94

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16269164, ECO:0007744|PDB:1YXH
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

219869

PDB entries from 2024-05-15

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