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2HZ4

Abl kinase domain unligated and in complex with tetrahydrostaurosporine

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
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 4ST B 501
ChainResidue
BLEU248
BLEU370
BASP381
BALA269
BLYS271
BTHR315
BGLU316
BPHE317
BMET318
BGLY321
BARG367

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4ST A 501
ChainResidue
ATRP235
ATRP261
ATYR264
ALYS294
ALEU302
CTYR342
CPHE497
CGLN498
CSER500

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 4ST C 501
ChainResidue
ATYR342
APHE497
AGLN498
ASER500
CTRP235
CTYR264
CGLN300
CLEU302

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 Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP363
BASP363
CASP363

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
ALEU248
ALYS271
AGLU316
BLEU248
BLYS271
BGLU316
CLEU248
CLYS271
CGLU316

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P42684
ChainResidueDetails
ASER229
BSER229
CSER229

site_idSWS_FT_FI4
Number of Residues9
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR253
ATYR257
ATYR413
BTYR253
BTYR257
BTYR413
CTYR253
CTYR257
CTYR413

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
ChainResidueDetails
ATYR393
BTYR393
CTYR393

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00520
ChainResidueDetails
ASER446
BSER446
CSER446

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP363
AARG367

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP363
BARG367

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP363
CARG367

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP363
AALA365

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP363
BALA365

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP363
CALA365

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN368
AASP363
AALA365

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN368
BASP363
BALA365

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN368
CASP363
CALA365

224201

PDB entries from 2024-08-28

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