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1KPM

First Structural Evidence of a Specific Inhibition of Phospholipase A2 by Vitamin E and its Implications in Inflammation: Crystal Structure of the Complex Formed between Phospholipase A2 and Vitamin E at 1.8 A Resolution.

Replaces:  1FE7
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
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
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
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE VIT A 401
ChainResidue
ALEU2
ACYS45
AHIS48
AASP49
ALYS69
AHOH508
AHOH517
BASN54
BCYS133
ALEU3
AGLY6
ALYS7
AALA18
AILE19
ATYR22
ASER23
ATYR28

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 501
ChainResidue
APRO121
BGLU11
BARG77
BARG107

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 502
ChainResidue
APRO121
APHE124
BARG107
BGLN108
BHOH540

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 503
ChainResidue
BTHR89
BSER90
BHOH596

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 504
ChainResidue
AARG43
AHOH537
AHOH641

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaIC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
AHIS48
AASP99
BHIS48
BASP99

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49
BTYR28
BGLY30
BGLY32
BASP49

218853

数据于2024-04-24公开中

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