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

5D12

Kinase domain of cSrc in complex with RL40

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 Residues9
Detailsbinding site for residue G97 A 601
ChainResidue
ALEU273
AGLY274
AMET338
AGLU339
ATYR340
AMET341
ASER342
AGLY344
ALEU393

site_idAC2
Number of Residues7
Detailsbinding site for residue G97 B 601
ChainResidue
BLEU273
BALA293
BGLU339
BTYR340
BMET341
BGLY344
BLEU393

site_idAC3
Number of Residues13
Detailsbinding site for Di-peptide ARG B 264 and PRO B 333
ChainResidue
AALA259
AASN287
BILE262
BPRO263
BGLU265
BSER266
BLEU267
BLEU297
BVAL329
BGLU331
BGLU332
BILE334
BTYR335

site_idAC4
Number of Residues7
Detailsbinding site for Di-peptide ALA B 327 and VAL B 337
ChainResidue
BTRP260
BTRP286
BLEU325
BTYR326
BVAL328
BILE336
BMET338

site_idAC5
Number of Residues8
Detailsbinding site for Di-peptide CYS B 345 and ASP B 348
ChainResidue
BGLY344
BLEU346
BLEU347
BPHE349
BLEU350
BGLY352
BALA390
BILE392

site_idAC6
Number of Residues8
Detailsbinding site for Di-peptide CYS B 345 and ASP B 348
ChainResidue
BGLY344
BLEU346
BLEU347
BPHE349
BLEU350
BGLY352
BALA390
BILE392

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP386
BASP386

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU273
BLEU273

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS295
BLYS295

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR416
BTYR416

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081
ChainResidueDetails
ATYR436
BTYR436

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721
ChainResidueDetails
ACYS498
BCYS498

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005
ChainResidueDetails
ATYR527
BTYR527

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon