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3HMN

Crystal structure of human Mps1 catalytic domain in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0005975biological_processcarbohydrate metabolic process
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP A 1
ChainResidue
AHOH6
AGLY605
AASP608
ALEU654
AILE531
AGLY532
ASER533
AGLY534
AVAL539
AALA551
AMET602
AGLU603

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 7PE A 1153
ChainResidue
ASER537
AVAL539
ALYS553
AMET600
AILE663

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGSSKVFqVlnekkqi...........YAIK
ChainResidueDetails
AILE531-LYS553

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHsDLKpaNFLI
ChainResidueDetails
AILE643-ILE655

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
AASP647

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS553
AILE531

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PDB entries from 2024-06-12

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