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1FIT

FHIT (FRAGILE HISTIDINE TRIAD PROTEIN)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001650cellular_componentfibrillar center
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006163biological_processpurine nucleotide metabolic process
A0006915biological_processapoptotic process
A0015964biological_processdiadenosine triphosphate catabolic process
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0042802molecular_functionidentical protein binding
A0043530molecular_functionadenosine 5'-monophosphoramidase activity
A0047352molecular_functionadenylylsulfate-ammonia adenylyltransferase activity
A0047627molecular_functionadenylylsulfatase activity
A0047710molecular_functionbis(5'-adenosyl)-triphosphatase activity
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PDB Data
site_idAVE
Number of Residues1
DetailsCATALYTIC HISTIDINE.
ChainResidue
AHIS96

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. QdgpeAgQtVkHVHVHVLP
ChainResidueDetails
AGLN83-PRO101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:15182206, ECO:0000269|PubMed:9323207
ChainResidueDetails
AHIS96

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9261067, ECO:0007744|PDB:3FIT
ChainResidueDetails
AHIS8

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9323207, ECO:0007744|PDB:5FIT
ChainResidueDetails
AASN27
AGLN83
AGLY89
AHIS98

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for induction of apoptosis => ECO:0000269|PubMed:16407838
ChainResidueDetails
ATYR114

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:15007172
ChainResidueDetails
ATYR114

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15007172
ChainResidueDetails
ATYR145

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 5fit
ChainResidueDetails
AGLN83
AHIS96
AHIS94

site_idMCSA1
Number of Residues4
DetailsM-CSA 101
ChainResidueDetails
AGLN83electrostatic stabiliser, hydrogen bond donor
AHIS94electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
AHIS96metal ligand, nucleofuge, nucleophile
AHIS98electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-05-08

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