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3FQH

Crystal structure of spleen tyrosine kinase complexed with a 2-substituted 7-azaindole

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 Residues11
DetailsBINDING SITE FOR RESIDUE 057 A 1
ChainResidue
ALEU377
ALEU501
AHOH1043
AGLY378
AALA400
AGLU449
AALA451
AGLU452
AGLY454
APRO455
ALYS458

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 057 B 2
ChainResidue
BGLY378
BSER379
BALA400
BGLU449
BALA451
BGLU452
BGLY454
BPRO455
BLYS458
BLEU501

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P48025","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18369315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP494
AARG498

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP494
BARG498

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP494
AALA496

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP494
BALA496

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP494
AASN499
AALA496

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP494
BASN499
BALA496

239149

PDB entries from 2025-07-23

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