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6PNX

Crystal Structure of an Asymmetric Dimer of FGF Receptor 3 Kinases Trapped in A-loop Tyrosine Transphosphorylation Reaction

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 Residues14
Detailsbinding site for residue ACP A 801
ChainResidue
ALEU478
AASN562
ALEU624
AHOH959
AHOH996
AHOH997
AGLU480
AGLY481
APHE483
AALA506
AVAL555
AGLU556
ATYR557
AALA558

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 802
ChainResidue
AASP593
ACYS597
AASN629

site_idAC3
Number of Residues14
Detailsbinding site for residue ACP B 801
ChainResidue
ATYR647
BLEU478
BGLY479
BGLU480
BGLY481
BGLU556
BTYR557
BALA558
BASN622
BLEU624
BASP635
BHOH904
BHOH962
BHOH978

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 802
ChainResidue
BLYS560
BPHE566
BARG570
BGLU586

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeaigidkdraakpvt...VAVK
ChainResidueDetails
ALEU478-LYS508

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS613-VAL625

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
ChainResidueDetails
AASP617
BASP617

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU478
ALYS508
BLEU478
BLYS508

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:8754806
ChainResidueDetails
ATYR647
ATYR648
BTYR647
BTYR648

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11294897
ChainResidueDetails
ATYR724
BTYR724

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PDB entries from 2024-07-31

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