Structure for peptidase homologue C26.952: dihydro-orotase (N-terminal unit) (Homo sapiens-type)

Summary Alignment Tree Sequences Sequence features Distribution Structure

 

TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
mature  peptidase 1.73 Å 4BY3 4BY3 4BY3 4BY3 4BY3 4BY3 Grande-Garcia et al., 2014
mature  peptidase 1.66 Å 4C6B 4C6B 4C6B 4C6B 4C6B 4C6B Grande-Garcia et al., 2014
mature  peptidase 1.45 Å 4C6C 4C6C 4C6C 4C6C 4C6C 4C6C Grande-Garcia et al., 2014
mature  peptidase 1.30 Å 4C6D 4C6D 4C6D 4C6D 4C6D 4C6D Grande-Garcia et al., 2014
mature  peptidase 1.26 Å 4C6E 4C6E 4C6E 4C6E 4C6E 4C6E Grande-Garcia et al., 2014
mature  peptidase 1.26 Å 4C6F 4C6F 4C6F 4C6F 4C6F 4C6F Grande-Garcia et al., 2014
mature  peptidase 1.35 Å 4C6I 4C6I 4C6I 4C6I 4C6I 4C6I Grande-Garcia et al., 2014
mature  peptidase 1.30 Å 4C6J 4C6J 4C6J 4C6J 4C6J 4C6J Grande-Garcia et al., 2014
mature  peptidase 1.48 Å 4C6K 4C6K 4C6K 4C6K 4C6K 4C6K Grande-Garcia et al., 2014
mature  peptidase 1.55 Å 4C6L 4C6L 4C6L 4C6L 4C6L 4C6L Grande-Garcia et al., 2014
mature  peptidase 1.62 Å 4C6M 4C6M 4C6M 4C6M 4C6M 4C6M Grande-Garcia et al., 2014
mature  peptidase 1.90 Å 4C6N 4C6N 4C6N 4C6N 4C6N 4C6N Grande-Garcia et al., 2014
mature  peptidase 1.65 Å 4C6O 4C6O 4C6O 4C6O 4C6O 4C6O Grande-Garcia et al., 2014
mature  peptidase 1.52 Å 4C6P 4C6P 4C6P 4C6P 4C6P 4C6P Grande-Garcia et al., 2014
mature  peptidase 1.66 Å 4C6Q 4C6Q 4C6Q 4C6Q 4C6Q 4C6Q Grande-Garcia et al., 2014
crystal structure of the dihydroorotase domain (k1556a) of human cad 2.77 Å 5YNZ 5YNZ 5YNZ 5YNZ 5YNZ 5YNZ
Phe1563Leu mutant; apo structure 1.87 Å 6HFD 6HFD 6HFD 6HFD 6HFD 6HFD
Phe1563Leu mutant; apo structure 1.48 Å 6HFE 6HFE 6HFE 6HFE 6HFE 6HFE
Phe1563Tyr mutant; apo structure 1.51 Å 6HFF 6HFF 6HFF 6HFF 6HFF 6HFF
Phe1563Ala mutant; co-crystallized with carbamoyl aspartate at ph 7.0 1.45 Å 6HFH 6HFH 6HFH 6HFH 6HFH 6HFH
Phe1563Ala mutant; apo structure 1.46 Å 6HFI 6HFI 6HFI 6HFI 6HFI 6HFI
Phe1563Ala mutant; co-crystallized with carbamoyl aspartate at ph 7.5 1.20 Å 6HFJ 6HFJ 6HFJ 6HFJ 6HFJ 6HFJ
Phe1563Leu mutant; co-crystallized with carbamoyl aspartate at ph 6.5 1.46 Å 6HFK 6HFK 6HFK 6HFK 6HFK 6HFK
Phe1563Leu mutant; co-crystallized with carbamoyl aspartate at ph 7.0 1.35 Å 6HFL 6HFL 6HFL 6HFL 6HFL 6HFL
Phe1563Leu mutant; co-crystallized with carbamoyl aspartate at ph 7.5 1.45 Å 6HFN 6HFN 6HFN 6HFN 6HFN 6HFN
Phe1563Thr mutant; co-crystallized with carbamoyl aspartate at ph 7.0 1.20 Å 6HFP 6HFP 6HFP 6HFP 6HFP 6HFP
Phe1563Thr mutant; co-crystallized with carbamoyl aspartate at ph 7.5 1.15 Å 6HFQ 6HFQ 6HFQ 6HFQ 6HFQ 6HFQ
Phe1563Tyr mutant; co-crystallized with carbamoyl aspartate at ph 7.0 1.30 Å 6HFR 6HFR 6HFR 6HFR 6HFR 6HFR
Phe1563Tyr mutant; co-crystallized with carbamoyl aspartate at ph 6.5 1.35 Å 6HFS 6HFS 6HFS 6HFS 6HFS 6HFS
Phe1563Tyr mutant; co-crystallized with carbamoyl aspartate at ph 7.5 1.40 Å 6HFU 6HFU 6HFU 6HFU 6HFU 6HFU
hybrid dihydroorotase domain of human cad with e. coli flexible loop in apo state 2.12 Å 6HG1 6HG1 6HG1 6HG1 6HG1 6HG1
hybrid dihydroorotase domain of human cad with e. coli flexible loop, bound to fluoroorotate 1.83 Å 6HG2 6HG2 6HG2 6HG2 6HG2 6HG2
hybrid dihydroorotase domain of human cad with e. coli flexible loop, bound to dihydroorotate 1.97 Å 6HG3 6HG3 6HG3 6HG3 6HG3 6HG3