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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 Residues251
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsMotif: {"description":"Kinase activation loop"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00520","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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