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6JUX

Crystal structure of human ALK2 kinase domain with R206H mutation in complex with RK-71807

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 Residues19
Detailsbinding site for residue C9U A 501
ChainResidue
AVAL214
ATYR285
AHIS286
AGLU287
AGLY289
AASP293
ALYS340
ALEU343
ASER463
AHOH606
AHOH631
ATYR219
AVAL222
AALA233
ALYS235
ALEU263
ALEU281
ATHR283
AHIS284

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 502
ChainResidue
AARG380
AASN437
AASP438
APRO439
AHOH620
AHOH661
AHOH693

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
AHIS286
ALYS345
ALYS346
AHOH607
AHOH613
AHOH660

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGRYGEVWrGswqgen............VAVK
ChainResidueDetails
AVAL214-LYS235

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV
ChainResidueDetails
AILE332-VAL344

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
AASP336

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL214
ALYS235

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PDB entries from 2024-07-17

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