Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4F65

Crystal structure of Human Fibroblast Growth Factor Receptor 1 Kinase domain in complex with compound 8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005007molecular_functionfibroblast growth factor receptor activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005007molecular_functionfibroblast growth factor receptor 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
AARG470
ATRP471
AGLU472
ALEU500
ALEU548
AEDO807

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AHOH957
AGLY539
ALYS540
ALYS618

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 803
ChainResidue
AARG470
ALYS618
AHIS679
AHOH963

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 804
ChainResidue
AGLN574
AARG577
AGLY697
AGLY698
ASER699

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 805
ChainResidue
AALA615
APHE747
ALYS748
AHOH974

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 807
ChainResidue
AARG470
ASO4801

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 0S9 A 808
ChainResidue
ALEU484
AGLU486
AGLY487
AVAL492
AALA512
ALYS514
AGLU531
AVAL561
AGLU562
ATYR563
AALA564
ASER565
AGLY567
AARG627
ALEU630
AHOH969
AHOH993

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BARG570
BARG627
BTHR657
BASN659
BARG661
BHOH902

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BSER597
BVAL601
BPHE694
BASN724
BCYS725
BTHR726
BLEU729

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 804
ChainResidue
BGLN574
BASN659
BARG661

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 805
ChainResidue
BPRO578

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 806
ChainResidue
BPRO466
BILE529
BGLU533
BTHR552

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 807
ChainResidue
AGLY703
AVAL704
BGLU708

site_idBC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0S9 B 808
ChainResidue
BLEU484
BGLU486
BALA512
BLYS514
BGLU531
BVAL561
BGLU562
BTYR563
BALA564
BSER565
BGLY567
BLEU630
BPHE642
BHOH960
BHOH981

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
ALEU484-LYS514

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS619-VAL631

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":"19224897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19665973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon