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2Q0B

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565A Mutation Responsible for Pfeiffer Syndrome

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AARG625
ALEU647
AARG649
AARG664
AHOH922
AHOH924
AHOH928

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
BVAL743
BPRO744
BSER745
AARG737
AHOH901

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACP A 803
ChainResidue
ALEU487
AALA515
AILE548
AALA565
AALA567
ALEU633

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
BARG625
BARG649
BARG664

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BTHR729
BASN730
BHOH901

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACP B 803
ChainResidue
BALA515
BALA565
BTYR566
BALA567
BLEU633

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...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
AALA565
AASN571
BLEU487
BLYS517
BALA565
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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
AARG630

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BARG630

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
AALA628

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BALA628

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR661
AASP626
AALA628

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR661
BASP626
BALA628

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP626
AALA628
AASN631

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP626
BALA628
BASN631

226707

PDB entries from 2024-10-30

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