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6V9C

Crystal structure of FGFR4 kinase domain in complex with covalent inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue QS7 A 801
ChainResidue
ALEU473
AGLY556
ALEU619
AALA629
AASP630
AHOH947
AVAL481
AARG483
ALYS503
AGLU520
AVAL550
AGLU551
ACYS552
AALA553

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 802
ChainResidue
AARG559
AARG616
ATHR646
ASER647
AASN648
AARG650
AHOH979

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 803
ChainResidue
AHIS727
AALA728
AHOH932

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVrAeafgmdparpdqast...VAVK
ChainResidueDetails
ALEU473-LYS503

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS608-VAL620

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
ATHR621

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU473
ALYS503

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY582

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18670643
ChainResidueDetails
ALEU651
APRO652

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PDB entries from 2024-07-17

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