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2PWL

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic N549H Mutation Responsible for Crouzon 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AHOH72
AHOH117
AARG625
ALEU647
AARG649
AARG664

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
BSER745
AARG737
BVAL743
BPRO744

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BARG625
BTHR660
BASN662
BARG664

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BHOH42
BTHR729
BASN730

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ACP A 300
ChainResidue
ALEU487
AGLY488
AGLY490
AALA491
AVAL495
AALA515
ALYS517
AVAL564
AGLU565
ATYR566
AALA567
ALEU633
AASP644

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ACP B 300
ChainResidue
BHOH33
BHOH92
BLEU487
BGLY488
BGLY490
BALA491
BVAL495
BALA515
BLYS517
BVAL564
BGLU565
BALA567
BASN571
BLEU633
BASP644

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
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 2024-04-10

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