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5UGL

Crystal Structure of FGF Receptor 2 Tyrosine Kinase Domain Harboring the D650V Activating Mutation

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 Residues4
Detailsbinding site for residue SO4 B 801
ChainResidue
BARG625
BARG649
BARG664
BTYR680

site_idAC2
Number of Residues14
Detailsbinding site for residue ANP B 802
ChainResidue
BGLU565
BALA567
BASN571
BARG630
BASN631
BLEU633
BASP644
BHOH955
BHOH978
BLEU487
BGLY488
BVAL495
BALA515
BVAL564

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 801
ChainResidue
AARG625
AARG649
ATYR656
ATHR660
AARG664

site_idAC4
Number of Residues15
Detailsbinding site for residue ANP A 802
ChainResidue
ALEU487
AGLY488
AVAL495
AALA515
ALYS517
AVAL564
AGLU565
AALA567
AARG630
AASN631
ALEU633
AASP644
AHOH903
AHOH954
AHOH970

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK
ChainResidueDetails
BLEU487-LYS517

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
BCYS622-VAL634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL495-ALA515
AVAL495-ALA515

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208
ChainResidueDetails
BVAL743
AVAL743

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
ChainResidueDetails
BVAL604
BVAL634
BHIS682
BSER688
AVAL604
AVAL634
AHIS682
ASER688

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
BGLY583
BPRO705
AGLY583
APRO705

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
BPRO703
APRO703

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PDB entries from 2025-06-11

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