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5MAH

Crystal structure of MELK in complex with an inhibitor

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 Residues19
Detailsbinding site for residue 7KD A 401
ChainResidue
AILE17
AGLU87
ATYR88
ACYS89
AGLU93
AGLU136
ALEU139
AILE149
AASP150
AHOH533
AHOH535
ATHR19
AGLY20
AALA23
AVAL25
AALA38
ALYS40
ACYS70
ALEU86

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 402
ChainResidue
AGLU35
AMET36
ATYR73
AGLU87
ATYR88
AGLU142
ALEU319
AALA322
AARG326
AHOH540

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 403
ChainResidue
AARG114
AGLU272

site_idAC4
Number of Residues3
Detailsbinding site for residue NA A 405
ChainResidue
AGLN181
ATRP273
AGLN274

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 Residues39
DetailsRegion: {"description":"UBA-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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 Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16216881","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
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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