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5ZV2

FGFR-1 in complex with ligand lenvatinib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005007molecular_functionfibroblast growth factor receptor activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005007molecular_functionfibroblast growth factor receptor activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue LEV A 801
ChainResidue
AGLY485
ALEU630
AASP641
APHE642
APHE489
AALA512
ALYS514
AGLU531
AMET535
AGLU562
AALA564
AGLY567

site_idAC2
Number of Residues15
Detailsbinding site for residue LEV B 801
ChainResidue
BLEU484
BGLY485
BPHE489
BALA512
BLYS514
BGLU531
BMET535
BVAL561
BGLU562
BTYR563
BALA564
BGLY567
BLEU630
BASP641
BPHE642

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
ALEU484-LYS514

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
ACYS619-VAL631

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:19224897
ChainResidueDetails
AASP623
BASP623

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ALEU484
BASN568
BARG627
BASP641
ALYS514
AGLU562
AASN568
AARG627
AASP641
BLEU484
BLYS514
BGLU562

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR463
ATYR583
ATYR585
BTYR463
BTYR583
BTYR585

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR653
ATYR654
BTYR653
BTYR654

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701
ChainResidueDetails
ATYR730
BTYR730

221371

PDB entries from 2024-06-19

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