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3DQW

c-Src kinase domain Thr338Ile mutant in complex with ATPgS

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
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AASN391
AASP404
AAGS534
AHOH717

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2
ChainResidue
BALA390
BASN391
BAGS534

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 3
ChainResidue
CASN391
CAGS534

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 4
ChainResidue
DASN391
DAGS534

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AGS A 534
ChainResidue
AMG1
AVAL281
AALA293
ALYS295
AILE338
AGLU339
AMET341
ASER345
AASP386
AASN391
ALEU393
AASP404
AHOH581
AHOH631
AHOH659
AHOH661
AHOH703
AHOH717

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AGS B 534
ChainResidue
BMG2
BVAL281
BALA293
BLYS295
BGLU310
BILE338
BGLU339
BMET341
BSER345
BASN391
BLEU393
BASP404
BGLY406
BHOH594
BHOH699

site_idAC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE AGS C 534
ChainResidue
CMG3
CLEU273
CGLY274
CGLY276
CPHE278
CVAL281
CALA293
CLYS295
CILE338
CGLU339
CMET341
CSER345
CLEU393
CASP404
CHOH535
CHOH570
CHOH590
CHOH598
CHOH620
CHOH634
CHOH635

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AGS D 534
ChainResidue
DMG4
DLEU273
DGLY276
DPHE278
DALA293
DLYS295
DILE338
DGLU339
DMET341
DSER345
DLEU393
DASP404
DHOH543
DHOH560
DHOH573
DHOH619
DHOH624

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGCFGEVWmGtwngttr...........VAIK
ChainResidueDetails
ALEU273-LYS295

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLRAANILV
ChainResidueDetails
ATYR382-VAL394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP386
BASP386
CASP386
DASP386

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU273
BLEU273
CLEU273
DLEU273

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS295
BLYS295
CLYS295
DLYS295

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081
ChainResidueDetails
APTR416
BPTR416
CPTR416
DPTR416

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR436
BTYR436
CTYR436
DTYR436

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721
ChainResidueDetails
ACYS498
BCYS498
CCYS498
DCYS498

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005
ChainResidueDetails
ATYR527
BTYR527
CTYR527
DTYR527

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP386
AALA390

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG388
BASN391
BASP386

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CARG388
CASN391
CASP386

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DARG388
DASN391
DASP386

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP386
BALA390

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP386
CALA390

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP386
DALA390

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG388
AASP386

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG388
BASP386

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CARG388
CASP386

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DARG388
DASP386

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG388
AASN391
AASP386

227111

PDB entries from 2024-11-06

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