Uniprot accession / id : P18440  OR   Uniprot accession / id : Q1JPA6  OR   Uniprot accession / id : Q78ZC4  OR   Uniprot accession / id : P50295  OR   Uniprot accession / id : Q45G59  OR   Uniprot accession / id : P50298  OR   Uniprot accession / id : P13914  OR   Uniprot accession / id : P13913  OR   Uniprot accession / id : P12275
 
Filter by :
Entry Information
Entry status  (1)
REL
(2)
 
Experimental methods  (1)
X-ray diffraction
(2)
 
Authors  (15)
Arrowsmith CH
(2)
Bochkarev A
(2)
Dombrovski L
(2)
Edwards AM
(2)
Grant DM
(2)
Loppnau P
(2)
Plotnikov AN
(2)
Structural Genomics Consortium (SGC)
(2)
Sundstrom M
(2)
Tempel W
(2)
Weigelt J
(2)
Wu H
(2)
Dombrovsky L
(1)
Goodfellow GH
(1)
Martin F
(1)
 
Homo / hetero assembly  (1)
homo
(2)
 
Assembly composition  (1)
protein structure
(2)
 
Assembly polymer count  (1)
monomer
(2)
 
Resolution distribution
1.5 - 2
(2)
 
Release year distribution
2005 - 2010
(2)
 
Journal  (2)
J Biol Chem
(1)
To be published
(1)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(2)
 
Organism name  (1)
Homo sapiens
(2)
 
Molecule name  (6)
Arylamide acetylase 1
(2)
Arylamine N-acetyltransferase 1
(2)
MNAT
(2)
Monomorphic arylamine N-acetyltransferase
(2)
N-acetyltransferase type 1
(2)
NAT-1
(2)
 
Molecule type  (1)
Protein
(2)
 
Gene names  (2)
AAC1
(2)
NAT1
(2)
 
Interacting ligands  (3)
ACM : ACETAMIDE
(1)
CL : CHLORIDE ION
(1)
NA : SODIUM ION
(1)
 
Function and Biology
EC number / name  (1)
2.3.1.5 : Arylamine N-acetyltransferase
(2)
 
Biological function  (5)
acetyltransferase activity
(2)
acyltransferase activity
(2)
arylamine N-acetyltransferase activity
(2)
protein binding
(2)
transferase activity
(2)
 
Biological process  (1)
xenobiotic metabolic process
(2)
 
Biological cell component  (2)
cytoplasm
(2)
cytosol
(2)
 
Sequence and Structure classification
CATH class  (1)
Alpha Beta
(2)
 
CATH topology  (1)
Arylamine N-acetyltransferase fold
(2)
 
Pfam accession / name  (1)
PF00797 : Acetyltransf_2
(2)
 
Experimental Information
Diffraction protocol  (2)
MAD
(1)
Single wavelength
(1)
 
Diffraction radiation source type  (2)
Rotating anode
(1)
Synchrotron
(1)
 
Diffraction source  (2)
NSLS BEAMLINE X25
(1)
RIGAKU FR-E+ DW
(1)
 
Representative Structures
Representative Structures
100%
95%
90%
70%
50%
40%
30%
Entries 1 to 2 of 2
Entries 1 to 2 of 2
 Select all entries on this page
Human N-acetyltransferase 1
Tempel W, Wu H, Dombrovski L, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Grant DM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)
J Biol Chem (2007) [PMID: 17656365  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: CL   
Modified residues: TYX    TYX   
Assembly name: Arylamine N-acetyltransferase 1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-148373 (Preferred)   search this ID
PDBe-KB: P18440   
X-ray diffraction
1.78Å resolution
Released: 15 May 2007
Model geometry
Fit model/data
2pqt
2pqt
2pqt
Human N-acetyltransferase 1 F125S mutant
Tempel W, Wu H, Dombrovski L, Loppnau P, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Grant DM, Bochkarev A, Plotnikov AN, Structural Genomics Consortium (SGC)
To be published
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: ACM    NA    ACM    NA   
Modified residues: MSE    MSE   
Assembly name: Arylamine N-acetyltransferase 1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-148373 (Preferred)   search this ID
PDBe-KB: P18440   
X-ray diffraction
1.701Å resolution
Released: 28 Nov 2006
Model geometry
Fit model/data
2ija
2ija
2ija
Entries 1 to 2 of 2
Entries 1 to 2 of 2