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3TKU

MRCK beta in complex with fasudil

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M77 A 418
ChainResidue
AILE82
ALEU207
APHE370
AGLY83
AVAL90
AALA103
AASP154
ATYR155
ATYR156
AASP204
AASN205

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE M77 A 419
ChainResidue
AHOH488
AHOH519

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 420
ChainResidue
APHE87
ALYS105
ALEU107
ACYS120
AGLU124
AGLY220

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE M77 B 418
ChainResidue
BILE82
BGLY83
BARG84
BVAL90
BALA103
BASP154
BTYR155
BTYR156
BASP204
BASN205
BLEU207
BPHE370

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE M77 B 419
ChainResidue
BHOH526

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 420
ChainResidue
BPHE87
BLYS105
BLEU107
BGLU124
BASP218
BGLY220

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVAvVkmknteri..........YAMK
ChainResidueDetails
AILE82-LYS105

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YvHrDIKpdNVLL
ChainResidueDetails
ATYR196-LEU208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues532
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P54265","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P54265","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q5VT25","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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