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4L68

Structure of the psedudokinase domain of BIR2, an immune regulator of the RLK/Pelle family

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 Residues4
DetailsBINDING SITE FOR RESIDUE PDO A 701
ChainResidue
AGLU397
ATHR402
APHE441
AHOH824

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE313
BLYS335
AILE313
ALYS335

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: Phosphoserine; by BAK1 => ECO:0000269|PubMed:24556575
ChainResidueDetails
ASER330
ASER389
ASER448
ASER462
BSER271
BSER286
BSER330
BSER389
BSER448
BSER462
ASER271
ASER286

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by BAK1 => ECO:0000269|PubMed:24556575
ChainResidueDetails
BTHR304
BTHR466
BTHR533
ATHR283
ATHR304
ATHR466
ATHR533
BTHR283

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q94AG2
ChainResidueDetails
BTHR402
BTHR482
ATHR402
ATHR482

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q94AG2
ChainResidueDetails
BTYR479
ATYR479

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q94AG2
ChainResidueDetails
BSER486
ASER486

219869

PDB entries from 2024-05-15

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