1I0X: Ribonuclease T1

Ribonuclease T1 in complex with 2'GMP (form II crystal). Determined by X-ray diffraction at 1.65 Å resolution. Released 14 Feb 2001.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Aspergillus oryzae
Chains: 4
Atoms: 3,750
Mol. weight: 46.4 kDa
Ligands: CA, 2GP
Released: 14 Feb 2001

Explore 1I0X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I0X contains 18 α-helices and 42 β-strands across 4 chains. 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

Element	Residues	Length	Sheet
β-strand	4-6	3	1
β-strand	9-11	3	1
α-helix	13-28	16
β-strand	33	1	2
β-strand	38	1	2
β-strand	40-42	3	3
β-strand	56-60	5	3
α-helix	66-68	3
β-strand	76-81	6	3
β-strand	86-91	6	3
β-strand	101-102	2	3

Chain B: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	4
β-strand	9-11	3	4
α-helix	13-29	17
β-strand	33	1	5
β-strand	38	1	5
β-strand	40-42	3	6
α-helix	53	1
α-helix	55	1
β-strand	56-60	5	6
β-strand	61	1	7
α-helix	66	1
β-strand	67	1	7
α-helix	68	1
β-strand	76-81	6	6
β-strand	86-91	6	6
β-strand	101-102	2	6

Chain C: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	8
β-strand	9-11	3	8
α-helix	13-29	17
β-strand	33	1	9
β-strand	38	1	9
β-strand	40-42	3	10
α-helix	53	1
α-helix	55	1
β-strand	56-60	5	10
β-strand	61	1	11
α-helix	66	1
β-strand	67	1	11
α-helix	68	1
β-strand	76-81	6	10
β-strand	86-91	6	10
α-helix	96-98	3
β-strand	101-102	2	10

Chain D: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	12
β-strand	9-11	3	12
α-helix	13-28	16
β-strand	33	1	13
β-strand	38	1	13
β-strand	40-42	3	14
α-helix	53	1
α-helix	55	1
β-strand	56-60	5	14
β-strand	61	1	15
α-helix	66	1
β-strand	67	1	15
α-helix	68	1
β-strand	76-81	6	14
β-strand	86-91	6	14
β-strand	101-102	2	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanyl-specific ribonuclease T1	A, B, C, D	protein	104	Aspergillus oryzae	P00651 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1I0X_1 GUANYL-SPECIFIC RIBONUCLEASE T1 (chains A, B, C, D)
ACDYTCGSNCYSSSDVSTAQAAGYKLHEDGETVGSNSYPHKYNNYEGFDFSVSSPYYEWP
ILSSGDVYSGGSPGADRVVFNENNQLAGVITHTGASGNNFVECT

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	5
2GP	Guanosine-2'-monophosphate	C10 H14 N5 O8 P	5

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:

1I0V 1.23 Å, Ribonuclease T1 in complex with 2'GMP (form I crystal)
4ODK 1.4 Å, Structure of SlyD from Thermus thermophilus in complex with T1 peptide
9RNT 1.5 Å, Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at…
1LOV 1.55 Å, X-ray structure of the E58A mutant of Ribonuclease T1 complexed with 3'-guanosine…
1LOY 1.55 Å, X-ray structure of the H40A/E58A mutant of Ribonuclease T1 complexed with 3'-guanosine…
4GSP 1.65 Å, Ribonuclease T1 complexed with 2',3'-cgps + 3'-GMP, 7 days
1HYF 1.7 Å, Ribonuclease T1 V16A mutant in complex with SR2+
1Q9E 1.7 Å, RNase T1 variant with adenine specificity
1RGA 1.7 Å, Crystal structure of RNase T1 with 3'-GMP and guanosine: a product complex
4BIR 1.7 Å, Ribonuclease T1: free HIS92GLN mutant
1I3I 1.76 Å, Ribonuclease T1 V78T mutant
3BU4 1.77 Å, Ribonuclease T1 complex with 2'GMP

Browse structure collections

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