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8X5K

The Crystal Structure of SYK from Biortus.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK
ChainResidueDetails
ALEU377-LYS402

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL
ChainResidueDetails
APHE490-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
AASP494

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU377
ALYS402

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR364
ATYR484
ATYR507
ATYR526
ATYR629
ATYR631

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ASER379
ASER579

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATHR384
ATHR530
ATHR582

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR525

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P48025
ChainResidueDetails
ATYR546

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR630

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PDB entries from 2024-11-13

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