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4J96

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer.

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
AARG577
AARG580
AGLY701

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FLC A 802
ChainResidue
AGLY663
AARG664
ALEU665
ALYS526
AARG625
AARG649
ATYR657
AMET659
ATHR660

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BARG577
BARG580
BGLY701
BSER702

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BTHR635
BASN637
BVAL639

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP B 803
ChainResidue
BLEU487
BGLY488
BGLU489
BGLY490
BALA491
BALA515
BVAL564
BGLU565
BTYR566
BALA567
BASN571
BLEU633
BASP644
BMG805
BHOH988
BHOH989
BHOH990

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FLC B 804
ChainResidue
BLYS526
BARG625
BARG649
BTYR657
BTHR660
BGLY663
BARG664

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 805
ChainResidue
BLYS517
BASP644
BACP803

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208
ChainResidueDetails
AASP626
BASP626

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
ChainResidueDetails
ALEU487
ALYS517
AGLU565
AASN571
BLEU487
BLYS517
BGLU565
BASN571

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
ATYR466
ATYR588
BTYR466
BTYR588

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
ATYR586
ATYR656
ATYR657
BTYR586
BTYR656
BTYR657

223532

PDB entries from 2024-08-07

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