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6VOV

Crystal structure of Syk in complex with GS-9876

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 R6D A 701
ChainResidue
ALEU377
AGLY454
ALEU501
AASP512
AHOH864
BASN615
AGLY378
AVAL385
AALA400
ALYS402
AMET448
AGLU449
AALA451
AGLU452

site_idAC2
Number of Residues13
Detailsbinding site for residue R6D B 701
ChainResidue
BLEU377
BGLY378
BPHE382
BVAL385
BALA400
BMET448
BGLU449
BALA451
BGLU452
BGLY454
BGLN462
BLEU501
BASP512

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP494
BASP494

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU377
ALYS402
BLEU377
BLYS402

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR364
BTYR526
BTYR629
BTYR631
ATYR484
ATYR507
ATYR526
ATYR629
ATYR631
BTYR364
BTYR484
BTYR507

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ASER379
ASER579
BSER379
BSER579

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATHR384
ATHR530
ATHR582
BTHR384
BTHR530
BTHR582

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR525
BTYR525

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P48025
ChainResidueDetails
ATYR546
BTYR546

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132
ChainResidueDetails
ATYR630
BTYR630

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PDB entries from 2024-11-06

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