Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1BUN

STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION

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
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0015459molecular_functionpotassium channel regulator activity
B0030414molecular_functionpeptidase inhibitor activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 121
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 122
ChainResidue
AASP39
AALA40
ALEU41
AGLU105

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRTAaLC
ChainResidueDetails
AVAL90-CYS100

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FryGGCngngnhFksdhlC
ChainResidueDetails
BPHE35-CYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
AARG75

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:8590005
ChainResidueDetails
AALA55
ALYS57
AHIS59
ATHR76

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP94

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon