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4QRC

Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 4 in Complex with Ponatinib

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AARG616
ATHR646
AASN648
AARG650
AHOH945
AHOH946
AHOH974

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 0LI A 802
ChainResidue
AVAL502
ALYS503
AGLU520
AMET524
AVAL550
AGLU551
ACYS552
AALA553
ALEU603
ACYS608
AILE609
AHIS610
AARG611
ALEU619
AILE628
AALA629
AASP630
APHE631
ALEU633
AVAL481
AALA501

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 803
ChainResidue
AARG563
AARG566
ASER688

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 804
ChainResidue
ALYS555
AGLU622
AASP623
AASN624

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 805
ChainResidue
AARG707
ATRP726
AHIS727
AALA728
AHOH938
AHOH989

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVrAeafgmdparpdqast...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
AASP612

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
ASER573

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18670643
ChainResidueDetails
ATYR642
ATYR643

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PDB entries from 2024-09-11

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