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5FRI

ALK5 in complex witha an N-(4-anilino-2-pyridyl)acetamide inhibitor.

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1499
ChainResidue
AASP269
AGLY271
ATHR272
ATRP273
AHOH2074

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1500
ChainResidue
AHOH2055
AHIS256
AGLU257
ATHR272
AGLU447

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ZUQ A 1501
ChainResidue
AILE211
AVAL219
AALA230
ALYS232
ASER280
AASP281
ATYR282
AHIS283
AGLU284
AGLY286
ATHR323
ALEU340
AASP351
AHOH2042
AHOH2094
AHOH2241

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP333

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE211
ALYS232

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250
ChainResidueDetails
ALYS391

219140

PDB entries from 2024-05-01

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