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5UI0

Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring an E565A/K659M Double Gain-of-Function 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 Residues6
Detailsbinding site for residue FLC A 801
ChainResidue
AARG625
AARG649
ATYR657
AMET659
AGLY663
AARG664

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 802
ChainResidue
AARG577
AARG580
AGLY701

site_idAC3
Number of Residues7
Detailsbinding site for residue FLC B 801
ChainResidue
BLYS526
BARG625
BARG649
BTYR657
BTHR660
BGLY663
BARG664

site_idAC4
Number of Residues18
Detailsbinding site for residue ACP B 802
ChainResidue
BLEU487
BGLY488
BPHE492
BGLY493
BALA515
BLYS517
BVAL564
BALA565
BTYR566
BALA567
BASN571
BASN631
BLEU633
BASP644
BHOH903
BHOH941
BHOH969
BHOH992

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK
ChainResidueDetails
ALEU487-LYS517

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS622-VAL634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL495-ALA515
BVAL495-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
AVAL743
BVAL743

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

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

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
APRO703
BPRO703

221716

PDB entries from 2024-06-26

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