Brand  (β version)

PDB ID: 6S1U

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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
0A1 O-methyl-L-tyrosine
PSA 3-hydroxy-4-amino-5-phenylpentanoic acid
Glycosylation
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Modification
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Structure summary

Code : 6S1U   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of dimeric M-PMV protease C7A/D26N/C106A mutant in complex with inhibitor
Release Data : 2019-10-16
Compound :
mol_id molecule chains synonym
1 Gag-Pro-Pol polyprotein A,B Pr180
ec: 3.6.1.23,3.4.23.-,2.7.7.49,2.7.7.7,3.1.26.4,2.7.7.-,3.1.-.-
mutation: C7A, D26N, C106A; ENGINEERED MUTATION
other_details: Gaps in the sequence indicate residues that were not modeled because of poor electron density.
mol_id molecule chains
2 PRO-0A1-VAL-PSA-ALA-MET-THR I
other_details: In the standard definition used by Refmac, the Cgamma atom of the PSA residue is labeled as CA. In the PDB Validation Report this label is interpreted as Calpha causing geometrical alerts. These alerts are false and should be ignored.
Source :
mol_id organism_scientific organism_common expression_system
1 Mason-Pfizer monkey virus  (taxid:11855) MPMV Escherichia coli 'BL21-Gold(DE3)pLysS AG'  (taxid:866768)
gene: gag-pro-pol
expression_system_plasmid: pBPS13ATG
mol_id organism_scientific
2 Synthetic construct  (taxid:32630)
synthetic: yes
Authors : Wosicki, S., Gilski, M., Jaskolski, M., Zabranska, H., Pichova, I.
Keywords : Mason-Pfizer Monkey Virus, M-PMV, retrovirus, retropepsin, aspartic protease, dimerization, inhibitor, flap structure, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Comparison of a retroviral protease in monomeric and dimeric states.

Wosicki, S.,Gilski, M.,Zabranska, H.  et al.
(2019)  Acta Crystallogr D Struct Biol  75 : 904 - 917

PubMed: 31588922
DOI: 10.1107/S2059798319011355

Crystal structure of a monomeric retroviral protease solved by protein folding game players.

Khatib, F.,DiMaio, F.,Cooper, S.  et al.
(2011)  Nat.Struct.Mol.Biol.  18 : 1175 - 1177

PubMed: 21926992
DOI: 10.1038/nsmb.2119

High-resolution structure of a retroviral protease folded as a monomer.

Gilski, M.,Kazmierczyk, M.,Krzywda, S.  et al.
(2011)  Acta Crystallogr.,Sect.D  67 : 907 - 914

PubMed: 22101816
DOI: 10.1107/S0907444911035943

Crystal structure of a retroviral protease proves relationship to aspartic protease family.

Miller, M.,Jaskolski, M.,Rao, J.K.  et al.
(1989)  Nature  337 : 576 - 579

PubMed: 2536902
DOI: 10.1038/337576a0

Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease.

Wlodawer, A.,Miller, M.,Jaskolski, M.  et al.
(1989)  Science  245 : 616 - 621

PubMed: 2548279

Reaction

Chain : A, B
UniProt : P07572 (POL_MPMV)
Reaction: EC: Evidence:
Physiological Direction:
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.49 PROSITE- ProRule:PRU00405, PubMed:22171253
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a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) 2.7.7.7 PROSITE- ProRule:PRU00405, PubMed:22171253
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Endonucleolytic cleavage to 5'-phosphomonoester. 3.1.26.4 PROSITE-ProRule:PRU00408
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dUTP + H2O = diphosphate + dUMP + H(+) 3.6.1.23 UniProtKB:P07570
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