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

6BL8

Predicting the Conformational Variability of Abl Tyrosine Kinase Using Molecular Dynamics Simulations and Markov State Models

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 Residues16
Detailsbinding site for residue PVB A 601
ChainResidue
ALEU248
AGLY321
AASN322
ALEU370
APHE382
AHOH710
AHOH798
AHOH808
AGLY250
AALA269
AVAL299
ATHR315
AGLU316
APHE317
AMET318
ATHR319

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 602
ChainResidue
ALYS245
AHIS246
ALYS247
AHOH702
AHOH725
BGLN477
BHOH703

site_idAC3
Number of Residues9
Detailsbinding site for residue PVB B 601
ChainResidue
BLEU248
BALA269
BTHR315
BGLU316
BPHE317
BMET318
BTHR319
BGLY321
BLEU370

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 B 602
ChainResidue
BARG362
BPHE393
BALA395
BHIS396
BHOH714

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 B 603
ChainResidue
BARG460
BGLU462
BGLY463

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
AASP363
BASP363

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALEU248
ALYS271
AGLU316
BLEU248
BLYS271
BGLU316

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR253
ATYR257
ATYR413
BTYR253
BTYR257
BTYR413

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
ChainResidueDetails
APHE393
BPHE393

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520
ChainResidueDetails
ASER446
BSER446

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon