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3SRV

Crystal structure of spleen tyrosine kinase (SYK) in complex with a diaminopyrimidine carboxamide inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE S19 A 1
ChainResidue
AGOL2
AARG498
AASN499
ALEU501
ASER511
AASP512
AHOH52
AHOH235
AALA400
AMET448
AGLU449
AALA451
AGLY454
APRO455

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 636
ChainResidue
AHOH76
AHOH202
AMET424
ALEU427
AARG434
AMET435
AHOH637

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
AS191
ALYS402
AASP494
AARG498
AASN499
AASP512

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 3
ChainResidue
ALYS458

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE S19 B 2
ChainResidue
BHOH52
BHOH199
BLEU377
BSER379
BALA400
BVAL433
BMET448
BGLU449
BMET450
BALA451
BGLY454
BPRO455
BARG498
BASN499
BLEU501
BSER511
BASP512

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 4
ChainResidue
BHOH32
BGLN461
BLYS571

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK
ChainResidueDetails
ALEU377-LYS402
BLEU377-LYS402

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL
ChainResidueDetails
APHE490-LEU502
BPHE490-LEU502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
BASP494

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU377
BLYS402

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132
ChainResidueDetails
BTYR364
BTYR484
BTYR507
BTYR526
BTYR629
BTYR631

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21469132
ChainResidueDetails
BSER379
BSER579

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132
ChainResidueDetails
BTHR384
BTHR530
BTHR582

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132
ChainResidueDetails
BTYR525

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P48025
ChainResidueDetails
BTYR546

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132
ChainResidueDetails
BTYR630

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PDB entries from 2024-10-30

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