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1IAS

CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETA RECEPTOR CRYSTALLIZED WITHOUT FKBP12

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
A0016020cellular_componentmembrane
B0004672molecular_functionprotein kinase activity
B0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
B0016020cellular_componentmembrane
C0004672molecular_functionprotein kinase activity
C0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
C0016020cellular_componentmembrane
D0004672molecular_functionprotein kinase activity
D0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
D0016020cellular_componentmembrane
E0004672molecular_functionprotein kinase activity
E0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
E0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 1
ChainResidue
EHIS283
ELYS342
ELYS343

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 2
ChainResidue
ELYS337
EARG377
ESER434
EASP435

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 4
ChainResidue
CLYS223
CGLN208
CARG221

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 5
ChainResidue
CLYS337
CARG377
CASP435

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 6
ChainResidue
BTYR282
BHIS283
BLYS342
BLYS343

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 9
ChainResidue
ATYR282
AHIS283
ALYS342
ALYS343

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 10
ChainResidue
CTYR282
CHIS283
CLYS342
CLYS343

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 11
ChainResidue
BARG221
BLYS223

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 12
ChainResidue
BLYS337
BARG377
BLEU426
BASP435
BPRO436

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 13
ChainResidue
DTYR282
DHIS283
DLYS342
DLYS343

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 14
ChainResidue
DLYS337
DARG377
DLEU426
DASP435
DPRO436

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 15
ChainResidue
DARG221
DLYS223

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 18
ChainResidue
AARG221
ALYS223

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 E 20
ChainResidue
EARG221
ELYS223

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 21
ChainResidue
ALYS337
AARG377
ALEU426
ASER434
AASP435
APRO436

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGRFGEVWrGkwrgee............VAVK
ChainResidueDetails
AILE211-LYS232

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV
ChainResidueDetails
AILE329-VAL341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP333
BASP333
CASP333
DASP333
EASP333

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE211
ELYS232
ALYS232
BILE211
BLYS232
CILE211
CLYS232
DILE211
DLYS232
EILE211

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER165
BSER165
CSER165
DSER165
ESER165

site_idSWS_FT_FI4
Number of Residues10
DetailsMOD_RES: Phosphothreonine; by TGFBR2 => ECO:0000269|PubMed:7774578
ChainResidueDetails
ATHR185
ETHR186
ATHR186
BTHR185
BTHR186
CTHR185
CTHR186
DTHR185
DTHR186
ETHR185

site_idSWS_FT_FI5
Number of Residues15
DetailsMOD_RES: Phosphoserine; by TGFBR2 => ECO:0000269|PubMed:7774578
ChainResidueDetails
ASER187
DSER187
DSER189
DSER191
ESER187
ESER189
ESER191
ASER189
ASER191
BSER187
BSER189
BSER191
CSER187
CSER189
CSER191

site_idSWS_FT_FI6
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250
ChainResidueDetails
ALYS391
BLYS391
CLYS391
DLYS391
ELYS391

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS337
AASP333

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ELYS335
EASP333

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR375
ALYS335
AASP333

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR375
BLYS335
BASP333

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR375
CLYS335
CASP333

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR375
DLYS335
DASP333

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ETHR375
ELYS335
EASP333

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN338
ALYS335
AASP333

site_idCSA17
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN338
BLYS335
BASP333

site_idCSA18
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN338
CLYS335
CASP333

site_idCSA19
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASN338
DLYS335
DASP333

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS337
BASP333

site_idCSA20
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASN338
ELYS335
EASP333

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS337
CASP333

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS337
DASP333

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ELYS337
EASP333

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS335
AASP333

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS335
BASP333

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS335
CASP333

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS335
DASP333

225681

PDB entries from 2024-10-02

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