1HZ1: Ribonuclease T1 V16A mutant

Ribonuclease T1 V16A mutant in complex with MG2+. Determined by X-ray diffraction at 1.8 Å resolution. Released 31 Jan 2001.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Aspergillus niger
Chains
1
Atoms
888
Mol. weight
11.45 kDa
Ligands
2GP, MG
Released
31 Jan 2001

Explore 1HZ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HZ1 contains 2 α-helices and 9 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix13-2917
β-strand3312
β-strand3812
β-strand40-4233
β-strand56-6053
α-helix67-682
β-strand76-8163
β-strand86-9163
β-strand101-10223

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribonuclease T1Aprotein104Aspergillus nigerP00651 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HZ1_1 RIBONUCLEASE T1 (chains A)
ACDYTCGSNCYSSSDASTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT

Ligands and cofactors

IDNameFormulaCopies
2GPGuanosine-2'-monophosphateC10 H14 N5 O8 P1
MGMagnesium ionMg1

Primary citation

The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution. Deswarte, J., De Vos, S., Langhorst, U. et al. Eur J Biochem (2001) 268:3993-4000. DOI 10.1046/j.1432-1327.2001.02310.x · PubMed

Other PDB entries of the same protein (UniProt P00651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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