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4AW2

Crystal structure of CDC42 binding protein kinase alpha (MRCK alpha)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 22E A 500
ChainResidue
AASP33
ALYS339
AHOH2099
AHOH2210
AILE36
ALYS68
AGLN69
AARG71
AHIS73
AGLN145
AASP146
AASP147

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1418
ChainResidue
ATYR56
ATRP59
AARG123
ALEU397
APRO398
AHOH2202

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1419
ChainResidue
ALYS106
ALEU108
AALA120
ACYS121
AGLU125
AGLY221
AHOH2063

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1420
ChainResidue
AALA104
ATYR156
ATYR157
AHOH2105

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1421
ChainResidue
AGLU29
AARG71
ACYS408
ALEU410
AHOH2206

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVAvVklknadkv..........FAMK
ChainResidueDetails
AILE83-LYS106

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YvHrDIKpdNILM
ChainResidueDetails
ATYR197-MET209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P54265, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP201

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P54265, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE83

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:9418861
ChainResidueDetails
ALYS106

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q5VT25
ChainResidueDetails
ASER222
ASER234

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:Q5VT25
ChainResidueDetails
ATHR240

219869

PDB entries from 2024-05-15

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