Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4UMP

Structure of MELK in complex with inhibitors

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
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 5QM D 1334
ChainResidue
DALA38
DGLU57
DGLU87
DCYS89
DLEU139
DILE149
DASP150
DHOH2034

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 5QM A 1334
ChainResidue
AALA38
AGLU57
AGLU87
ACYS89
ALEU139
AILE149
AASP150
AHOH2043
AILE17

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 5QM B 1334
ChainResidue
BILE17
BALA38
BGLU57
BGLU87
BCYS89
BILE149
BASP150
BHOH2043

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5QM C 1334
ChainResidue
CILE17
CVAL25
CALA38
CGLU57
CGLU87
CCYS89
CLEU139
CILE149
CASP150
CHOH2036

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchiltgem..........VAIK
ChainResidueDetails
AILE17-LYS40

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF
ChainResidueDetails
ATYR128-PHE140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsRegion: {"description":"UBA-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16216881","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"16216881","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon