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4NTY

Cesium sites in the crystal structure of acid-sensing ion channel in complex with snake toxin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005272molecular_functionsodium channel activity
A0006814biological_processsodium ion transport
A0015280molecular_functionligand-gated sodium channel activity
A0016020cellular_componentmembrane
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0010466biological_processnegative regulation of peptidase activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
B0099106molecular_functionion channel regulator activity
C0004623molecular_functionphospholipase A2 activity
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0016787molecular_functionhydrolase activity
C0035821biological_processmodulation of process of another organism
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0050482biological_processarachidonic acid secretion
C0090729molecular_functiontoxin activity
C0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CS A 501
ChainResidue
ATYR68

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS A 503
ChainResidue
ATHR295
AGLU299
ATYR301
AASP302

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS A 504
ChainResidue
AASP238
ATHR240
APE4513
AHOH657

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 505
ChainResidue
ATYR110
AHIS111
ATYR123

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS A 506
ChainResidue
ALEU375
ALEU375
ALEU375

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CS A 507
ChainResidue
ALYS373
ALYS373
ALYS373
AHOH654
AHOH654
AHOH654

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS A 508
ChainResidue
AVAL319
AGLU320
AASN323
CASN3

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS A 510
ChainResidue
AGLU183
APHE185

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 512
ChainResidue
ALYS212
AARG310
AHOH604

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PE4 A 513
ChainResidue
ALEU96
AGLU98
AARG191
AASP238
AASP350
AGLU354
ACS504
AHOH667
AHOH668

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS B 101
ChainResidue
BGLN45
BHIS47
BPHE48
BHOH203

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS B 102
ChainResidue
CASP31
CSER32

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CS C 201
ChainResidue
BSER29
CPHE68
CHOH304

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CS C 202
ChainResidue
CSER80
CASN82

Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. CYEDPPF
ChainResidueDetails
BCYS7-PHE13

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCNCDRTAtLC
ChainResidueDetails
CVAL90-CYS100

site_idPS01206
Number of Residues21
DetailsASC Amiloride-sensitive sodium channels signature. YsiTaCridCeTryLVenCnC
ChainResidueDetails
ATYR304-CYS324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:22094702
ChainResidueDetails
BPCA1

site_idSWS_FT_FI2
Number of Residues355
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ALEU71-GLU426

site_idSWS_FT_FI3
Number of Residues26
DetailsTRANSMEM: Discontinuously helical
ChainResidueDetails
AVAL427-PHE453

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for channel gating
ChainResidueDetails
ATYR72
ATRP288

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for channel desensitizing
ChainResidueDetails
AGLU80

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900
ChainResidueDetails
AASN367
AASN394

224004

PDB entries from 2024-08-21

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