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5UHN

Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring a N549H/E565A 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 Residues3
Detailsbinding site for residue SO4 A 801
ChainResidue
AARG625
AARG649
ATYR656

site_idAC2
Number of Residues12
Detailsbinding site for residue ACP A 802
ChainResidue
AALA565
AALA567
AASN571
AASP644
AMG803
BALA491
ALEU487
AGLY488
AGLU489
AGLY490
AALA515
ALYS517

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 803
ChainResidue
AARG630
AASN631
AASP644
AACP802

site_idAC4
Number of Residues1
Detailsbinding site for residue SO4 B 801
ChainResidue
BARG625

site_idAC5
Number of Residues16
Detailsbinding site for residue ACP B 802
ChainResidue
BLEU487
BGLU489
BGLY490
BALA491
BPHE492
BGLY493
BALA515
BVAL564
BALA565
BTYR566
BALA567
BASN571
BASN631
BLEU633
BASP644
BMG803

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 803
ChainResidue
BARG630
BASN631
BASP644
BACP802

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
AGLN494-VAL514
BGLN494-VAL514

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
AALA742
BALA742

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
ChainResidueDetails
ALEU603
ALEU633
ATHR681
ATRP687
BLEU603
BLEU633
BTHR681
BTRP687

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
APRO582
ATYR704
BPRO582
BTYR704

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
ASER702
BSER702

218853

PDB entries from 2024-04-24

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