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

4YC8

C-Helix-Out Binding of Dasatinib Analog to c-Abl Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 4B7 A 601
ChainResidue
ALEU248
AMET318
ATHR319
ATYR320
AGLY321
ALEU370
APHE382
AALA269
ALYS271
APHE283
AMET290
AILE313
ATHR315
AGLU316
APHE317

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 602
ChainResidue
AHIS361
AASP363
AASN368
AALA380
APHE382
AGLY383

site_idAC3
Number of Residues6
Detailsbinding site for residue MES A 603
ChainResidue
AARG367
APRO402
AILE403
ALYS404
ATRP405
ALEU445

site_idAC4
Number of Residues10
Detailsbinding site for residue 4B7 B 601
ChainResidue
BALA269
BLYS271
BILE313
BTHR315
BGLU316
BPHE317
BMET318
BTHR319
BGLY321
BPHE382

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO B 602
ChainResidue
BHIS361
BARG362
BGLY383
BSER385

site_idAC6
Number of Residues5
Detailsbinding site for residue MES B 603
ChainResidue
BARG367
BPRO402
BILE403
BLYS404
BLEU445

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK
ChainResidueDetails
ALEU248-LYS271

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV
ChainResidueDetails
APHE359-VAL371

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
AALA344
BALA344

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ASER229
AGLN252
AASN297
BSER229
BGLN252
BASN297

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ALYS234
AGLU238
ATHR394
BLYS234
BGLU238
BTHR394

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
ChainResidueDetails
AASN374
BASN374

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520
ChainResidueDetails
AVAL427
BVAL427

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon