Structure of PDB 1fit Chain A

Receptor sequence

>1fitA (length=126) Species: 9606 (Homo sapiens) [Search protein sequence]

SFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLR
PDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLP
RKAGDASWRSEEEMAAEAAALRVYFQ

3D structure

PDB

1fit MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family.

Chain

Resolution

1.85 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Q83 H94 H96 H98
Catalytic site (residue number reindexed from 1)	Q82 H93 H95 H97
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	H71 F72 H73

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:1fit, PDBe:1fit, PDBj:1fit
PDBsum	1fit
PubMed	9261067
UniProt	P49789\|FHIT_HUMAN Bis(5'-adenosyl)-triphosphatase (Gene Name=FHIT)