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2OWB

Structure of the Catalytic Domain of Human Polo-like Kinase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS93
ACYS212
ACYS255
AACT502

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 502
ChainResidue
AZN501
AHIS93
AGLN94
ALYS97
ACYS212
ALEU256

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
ALYS178
ALEU179
AGLY180
AASN216
ATYR217
AHOH624
AHOH674

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 626 A 500
ChainResidue
AARG57
APHE58
ALEU59
AGLY62
AALA65
ALYS66
ACYS67
AALA80
ALYS82
AGLU131
ACYS133
AARG134
AARG136
APHE183
AHOH514
AHOH538
AHOH545

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFAKCFeIsdadtkev..........FAGK
ChainResidueDetails
ALEU59-LYS82

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKlgNLFL
ChainResidueDetails
AVAL172-LEU184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues252
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues27
DetailsRegion: {"description":"Activation loop"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18615013","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12207013","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by AURKA","evidences":[{"source":"PubMed","id":"12207013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18615013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLY180
AASP176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS178
AASP176

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR214
ALYS178
AASP176

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN181
ALYS178
AASP176

239803

PDB entries from 2025-08-06

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