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4D2T

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 Residues10
DetailsBINDING SITE FOR RESIDUE 3I7 D 1334
ChainResidue
DILE17
DHOH2021
DALA38
DGLU87
DTYR88
DCYS89
DPRO90
DGLY92
DLEU139
DILE149

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3I7 A 1334
ChainResidue
AALA23
AVAL25
ALEU27
AALA38
ALYS40
AGLU57
ACYS70
AGLU87
ATYR88
ACYS89
APRO90
AILE149
AASP150

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3I7 B 1334
ChainResidue
BILE17
BLEU27
BALA38
BGLU87
BCYS89
BPRO90
BILE149
BHOH2028

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3I7 C 1334
ChainResidue
BGLY18
BTHR19
CILE17
CALA38
CLYS40
CGLU87
CTYR88
CCYS89
CPRO90
CGLU93
CILE149

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

246704

PDB entries from 2025-12-24

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