Structure of PDB 3fit Chain A

Receptor sequence

>3fitA (length=124) Species: 9606 (Homo sapiens) [Search protein sequence]

MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDL
RPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVL
PRKAGDWRSEEEMAAEAAALRVYF

3D structure

PDB

3fit MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family.

Chain

Resolution

2.4 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

Enzymatic activity

Catalytic site (original residue number in PDB)	Q83 H94 H96 H98
Catalytic site (residue number reindexed from 1)	Q83 H94 H96 H98
Enzyme Commision number	2.7.7.51: adenylylsulfate--ammonia adenylyltransferase. 3.6.1.29: bis(5'-adenosyl)-triphosphatase. 3.6.2.1: adenylylsulfatase. 3.9.1.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FRU	A	H72 F73 H74	H72 F73 H74
BS02	A	A	H8 I10 N27 T91	H8 I10 N27 T91

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0003824	catalytic activity
GO:0005515	protein binding
GO:0016740	transferase activity
GO:0016787	hydrolase activity
GO:0031625	ubiquitin protein ligase binding
GO:0042802	identical protein binding
GO:0043530	adenosine 5'-monophosphoramidase activity
GO:0047352	adenylylsulfate-ammonia adenylyltransferase activity
GO:0047627	adenylylsulfatase activity
GO:0047710	bis(5'-adenosyl)-triphosphatase activity

	Biological Process
GO:0006163	purine nucleotide metabolic process
GO:0006915	apoptotic process
GO:0015964	diadenosine triphosphate catabolic process
GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0072332	intrinsic apoptotic signaling pathway by p53 class mediator

External links

PDB	RCSB:3fit, PDBe:3fit, PDBj:3fit
PDBsum	3fit
PubMed	9261067
UniProt	P49789\|FHIT_HUMAN Bis(5'-adenosyl)-triphosphatase (Gene Name=FHIT)