1fo6 Summary

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CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

The structure was published by Wang, W.C., Hsu, W.H., Chien, F.T., and Chen, C.Y., in 2001 in a paper entitled "Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 2000.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE Q44185 (1-304) (DCAS_RHIRD)search Agrobacterium tumefacienssearch 100% 304 99%
B N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE Q44185 (1-304) (DCAS_RHIRD)search Agrobacterium tumefacienssearch 100% 304 99%
C N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE Q44185 (1-304) (DCAS_RHIRD)search Agrobacterium tumefacienssearch 100% 304 99%
D N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE Q44185 (1-304) (DCAS_RHIRD)search Agrobacterium tumefacienssearch 100% 304 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q44185 (1 - 304) N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE Agrobacterium tumefaciens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (Q44185) Carbamilasesearch Nitrilase/N-carbamoyl-D-aminoacid amidohydrolasesearch PF00795: Carbon-nitrogen hydrolasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D (Q44185) hydrolase activity, acting on carbon-nitrogen (but not peptide) bondssearch N-carbamoyl-D-amino acid hydrolase activitysearch hydrolase activitysearch nitrogen compound metabolic processsearch

Chain InterPro annotation
A, B, C, D Carbon-nitrogen hydrolasesearch