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2V5Q

CRYSTAL STRUCTURE OF WILD-TYPE PLK-1 KINASE DOMAIN IN COMPLEX WITH A SELECTIVE DARPIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:18615013
ChainResidueDetails
AASP176
BASP176

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALEU59
BASP194
ALYS82
AGLU131
ALYS178
AASP194
BLEU59
BLYS82
BGLU131
BLYS178

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER103
BSER103

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:12207013
ChainResidueDetails
ASER137
BSER137

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR210
BTHR210

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR214
BTHR214

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250
ChainResidueDetails
ASER269
BSER269

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12442251
ChainResidueDetails
ASER335
BSER335

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS338
BLYS338

217705

PDB entries from 2024-03-27

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