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3RI1

Crystal structure of the catalytic domain of FGFR2 kinase in complex with ARQ 069

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 Residues10
DetailsBINDING SITE FOR RESIDUE 3RH A 2
ChainResidue
ASO46
ALEU633
AHOH229
AHOH324
AVAL495
AALA515
AGLU534
AVAL564
AGLU565
AALA567

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AHOH308
ATHR635
AASN637
AVAL639

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 7
ChainResidue
AHOH194
AHOH215
AARG625
AARG649
ATHR660
ATHR661
AASN662
AGLY663
AARG664

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AHOH127
ATHR681
AHIS682
AGLN683
BARG612

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 11
ChainResidue
AHOH58
AARG580
AGLY701
ASER702

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 6
ChainResidue
A3RH2
AHOH145
AHOH172
AHOH286
AHOH309
AGLU489
AGLY490
ACYS491
APHE492
AGLY493

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3RH B 1
ChainResidue
BHOH326
BHOH419
BVAL495
BALA515
BLYS517
BVAL564
BGLU565
BALA567
BLEU633
BSO4769

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 9
ChainResidue
AHOH76
BHOH226
BVAL709
BGLU710

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 8
ChainResidue
BHOH213
BHOH330
BARG625
BTHR660
BASN662
BGLY663
BARG664

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 769
ChainResidue
B3RH1
BHOH416
BGLU489
BGLY490
BCYS491
BPHE492
BGLY493

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 5
ChainResidue
BHOH137
BHOH205
BARG577
BARG580
BGLY700
BGLY701
BSER702

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
ALEU487
ALYS517
AGLU565
AASN571
BLEU487
BLYS517
BGLU565
BASN571

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
ATYR586
ATYR656
ATYR657
BTYR586
BTYR656
BTYR657

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PDB entries from 2024-07-17

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