Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7P8P

Crystal structure of Fhit covalently bound to a nucleotide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006163	biological_process	purine nucleotide metabolic process
A	0006351	biological_process	DNA-templated transcription
A	0006915	biological_process	apoptotic process
A	0015964	biological_process	diadenosine triphosphate catabolic process
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0042802	molecular_function	identical protein binding
A	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
A	0047352	molecular_function	adenylylsulfate-ammonia adenylyltransferase activity
A	0047627	molecular_function	adenylylsulfatase activity
A	0047710	molecular_function	bis(5'-adenosyl)-triphosphatase activity
A	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006163	biological_process	purine nucleotide metabolic process
B	0006351	biological_process	DNA-templated transcription
B	0006915	biological_process	apoptotic process
B	0015964	biological_process	diadenosine triphosphate catabolic process
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
B	0042802	molecular_function	identical protein binding
B	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
B	0047352	molecular_function	adenylylsulfate-ammonia adenylyltransferase activity
B	0047627	molecular_function	adenylylsulfatase activity
B	0047710	molecular_function	bis(5'-adenosyl)-triphosphatase activity
B	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006163	biological_process	purine nucleotide metabolic process
C	0006351	biological_process	DNA-templated transcription
C	0006915	biological_process	apoptotic process
C	0015964	biological_process	diadenosine triphosphate catabolic process
C	0016740	molecular_function	transferase activity
C	0016787	molecular_function	hydrolase activity
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
C	0042802	molecular_function	identical protein binding
C	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
C	0047352	molecular_function	adenylylsulfate-ammonia adenylyltransferase activity
C	0047627	molecular_function	adenylylsulfatase activity
C	0047710	molecular_function	bis(5'-adenosyl)-triphosphatase activity
C	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006163	biological_process	purine nucleotide metabolic process
D	0006351	biological_process	DNA-templated transcription
D	0006915	biological_process	apoptotic process
D	0015964	biological_process	diadenosine triphosphate catabolic process
D	0016740	molecular_function	transferase activity
D	0016787	molecular_function	hydrolase activity
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0032435	biological_process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
D	0042802	molecular_function	identical protein binding
D	0043530	molecular_function	adenosine 5'-monophosphoramidase activity
D	0047352	molecular_function	adenylylsulfate-ammonia adenylyltransferase activity
D	0047627	molecular_function	adenylylsulfatase activity
D	0047710	molecular_function	bis(5'-adenosyl)-triphosphatase activity
D	0072332	biological_process	intrinsic apoptotic signaling pathway by p53 class mediator

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Motif: {"description":"Histidine triad motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00464","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"15182206","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9323207","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9261067","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FIT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9323207","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FIT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15007172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	214
Details	Domain: {"description":"HIT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00464","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Important for induction of apoptosis","evidences":[{"source":"PubMed","id":"16407838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"15007172","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 101

Chain	Residue	Details
A	GLN83	electrostatic stabiliser, hydrogen bond donor
A	HIS94	electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
A	ASN96	metal ligand, nucleofuge, nucleophile
A	HIS98	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 101

Chain	Residue	Details
B	GLN83	electrostatic stabiliser, hydrogen bond donor
B	HIS94	electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
B	ASN96	metal ligand, nucleofuge, nucleophile
B	HIS98	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 101

Chain	Residue	Details
C	GLN83	electrostatic stabiliser, hydrogen bond donor
C	HIS94	electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
C	ASN96	metal ligand, nucleofuge, nucleophile
C	HIS98	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 101

Chain	Residue	Details
D	GLN83	electrostatic stabiliser, hydrogen bond donor
D	HIS94	electrostatic stabiliser, increase electrophilicity, increase nucleophilicity
D	ASN96	metal ligand, nucleofuge, nucleophile
D	HIS98	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)