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3GQI

Crystal Structure of activated receptor tyrosine kinase in complex with substrates

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005007molecular_functionfibroblast growth factor receptor activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DVT A 1
ChainResidue
AASP503
BARG694
BARG696
BASN697
BGLU698
ALYS504
APRO505
AASN506
AARG507
BHOH34
BLEU673
BTHR674
BARG675

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP A 775
ChainResidue
ALEU484
AGLY485
AGLY487
AALA488
APHE489
AGLY490
AVAL492
AALA512
ALYS514
AGLU562
AALA564
AASN568
AARG627
AASN628
ALEU630
AASP641
AMG776

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 776
ChainResidue
AASN628
AASP641
AACP775

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
ALEU484-LYS514

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS619-VAL631

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, ECO:0000269|PubMed:19224897
ChainResidueDetails
AASP623

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALEU484
ALYS514
AGLU562
AASN568
AARG627
AASP641

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Mediates interaction with PLCG1 and SHB
ChainResidueDetails
APTR766

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR463
APHE583
APHE585

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701
ChainResidueDetails
APTR653
APTR654

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR730

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19665973
ChainResidueDetails
APTR766

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG627
AASP623

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA625
AASP623

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR658
AALA625
AASP623

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN628
AALA625
AASP623

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PDB entries from 2024-05-01

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