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5O2B

Crystal structure of WNK3 kinase domain in a diphosphorylated state and in a complex with the inhibitor PP-121

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 PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue KS1 A 501
ChainResidue
ALYS159
AHOH660
AHOH710
AVAL161
AALA174
ACYS176
ATHR227
AGLU228
AMET230
APHE282
AASP294

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 502
ChainResidue
AASP150
AHOH614
AHOH673
AHOH688

site_idAC3
Number of Residues12
Detailsbinding site for residue KS1 B 501
ChainResidue
BGLY154
BLYS159
BVAL161
BALA174
BCYS176
BTHR227
BGLU228
BMET230
BPHE282
BASP294
BHOH650
BHOH657

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI
ChainResidueDetails
AILE271-ILE283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9JIH7
ChainResidueDetails
AASP294
BASP294

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9H4A3
ChainResidueDetails
ATHR227
ALYS277
BTHR227
BLYS277

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9JIH7
ChainResidueDetails
ASER304
BSER304

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:33439774
ChainResidueDetails
ASER308
BSER308

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PDB entries from 2024-09-04

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