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6AGX

The cocrystal structure of FGFR2 bound with compound 14 harboring 5H-pyrrolo[2,3-b]pyrazine scaffold

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 9WX A 800
ChainResidue
ALEU487
AALA643
AASP644
APHE645
AGLY488
ALYS517
AGLU534
AILE548
AALA567
AARG630
AASN631
ALEU633

site_idAC2
Number of Residues14
Detailsbinding site for residue 9WX B 800
ChainResidue
BLEU487
BGLY488
BGLY490
BGLY493
BALA515
BLYS517
BGLU534
BILE548
BVAL564
BALA567
BLEU633
BALA643
BASP644
BPHE645

site_idAC3
Number of Residues15
Detailsbinding site for residue 9WX C 800
ChainResidue
CLEU487
CGLY488
CALA515
CLYS517
CGLU534
CILE548
CVAL562
CVAL564
CTYR566
CALA567
CARG630
CLEU633
CALA643
CASP644
CPHE645

site_idAC4
Number of Residues13
Detailsbinding site for residue 9WX D 800
ChainResidue
DLEU487
DGLY488
DALA515
DLYS517
DGLU534
DILE548
DVAL564
DALA567
DARG630
DLEU633
DALA643
DASP644
DPHE645

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. CIHrDLTARNVLV
ChainResidueDetails
ACYS622-VAL634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"17803937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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