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4J98

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659Q 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 SO4 A 801
ChainResidue
AARG625
AARG649
ATYR657
AARG664
AHOH1004
AHOH1005

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AARG577
AARG580
AGLY701

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BARG625
BARG649
BTYR657
BTHR660
BARG664
BHOH904
BHOH1003
BHOH1004

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BARG577
BARG580
BSER702

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 803
ChainResidue
BTHR635
BASN637
BVAL639

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP B 804
ChainResidue
BLEU487
BGLY488
BGLU489
BGLY490
BALA491
BALA515
BVAL564
BGLU565
BTYR566
BALA567
BASN571
BASN631
BLEU633
BASP644
BHOH901
BHOH936
BHOH964

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"17803937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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