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7KIA

Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 19

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 PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVmAeavgidkdkpkeavt...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

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PDB entries from 2024-11-06

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