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1SNU

CRYSTAL STRUCTURE OF THE UNPHOSPHORYLATED INTERLEUKIN-2 TYROSINE KINASE CATALYTIC DOMAIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STU A 301
ChainResidue
AHOH176
ACYS442
AARG486
ALEU489
ASER499
AASP500
BHOH42
BPHE365
AILE369
AALA389
ALYS391
APHE435
AGLU436
APHE437
AMET438
AGLY441

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STU B 621
ChainResidue
BILE369
BGLY370
BVAL377
BALA389
BLYS391
BPHE435
BGLU436
BPHE437
BMET438
BGLY441
BCYS442
BARG486
BASN487
BLEU489
BSER499
BASP500

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGQFGLVHlGywlnkdk...........VAIK
ChainResidueDetails
AILE369-LYS391

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VIHrDLAARNCLV
ChainResidueDetails
AVAL478-VAL490

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP482
BASP482

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE369
ALYS391
BILE369
BLYS391

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by LCK => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR512
BTYR512

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER565
BSER565

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP482
AARG486

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP482
BARG486

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP482
AALA484

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP482
BALA484

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP482
AASN487
AALA484

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP482
BASN487
BALA484

222036

PDB entries from 2024-07-03

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