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6LVK

Crystal structure of FGFR2 in complex with 1,3,5-triazine derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue EVC A 801
ChainResidue
ALYS485
AGLY570
AGLU574
AARG630
ALEU633
AHOH912
AHOH915
AHOH921
ALEU487
AVAL495
AALA515
ALYS517
AGLU565
ATYR566
AALA567
ASER568

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 802
ChainResidue
AARG625
AARG649
ATHR660
AARG664

site_idAC3
Number of Residues18
Detailsbinding site for residue EVC B 801
ChainResidue
BLYS485
BLEU487
BPHE492
BALA515
BLYS517
BGLU565
BTYR566
BALA567
BSER568
BGLY570
BGLU574
BARG630
BASN631
BLEU633
BALA643
BHOH911
BHOH912
BHOH934

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 B 802
ChainResidue
BARG625
BARG649
BARG664
BHOH901
BHOH902
BHOH903
BHOH918

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 803
ChainResidue
AVAL743
APRO744
ASER745
BARG737

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 804
ChainResidue
BTHR635
BGLU636
BASN637
BVAL639

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. CIHrDLAARNVLV
ChainResidueDetails
ACYS622-VAL634

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208
ChainResidueDetails
AASP626
BASP626

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208
ChainResidueDetails
AGLU565
AASN571
BLEU487
BLYS517
BGLU565
BASN571
ALEU487
ALYS517

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
ATYR466
ATYR588
BTYR466
BTYR588

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646
ChainResidueDetails
BTYR656
BTYR657
ATYR586
ATYR656
ATYR657
BTYR586

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PDB entries from 2024-06-12

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