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

3JS2

Crystal structure of minimal kinase domain of fibroblast growth factor receptor 1 in complex with 5-(2-thienyl)nicotinic acid

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 Residues8
DetailsBINDING SITE FOR RESIDUE VM1 A 801
ChainResidue
AHOH132
ALEU484
AILE545
AVAL561
AGLU562
ATYR563
AALA564
ALEU630

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AHOH144
AARG570
AARG627
ATHR657
AASN659
AARG661
AHOH37

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VM1 B 801
ChainResidue
BLEU484
BVAL492
BGLU562
BTYR563
BALA564
BLEU630

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 2
ChainResidue
BHOH5
BHOH143
BARG570
BARG627
BTHR657
BASN659
BARG661

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

244349

PDB entries from 2025-11-05

PDB statisticsPDBj update infoContact PDBjnumon