Structure of PDB 1rds Chain A

Receptor sequence
>1rdsA (length=105) Species: 5063 (Aspergillus phoenicis) [Search protein sequence]
ESCEYTCGSTCYWSSDVSAAKAKGYSLYESGDTIDDYPHEYHDYEGFDFP
VSGTYYEYPIMSDYDVYTGGSPGADRVIFNGDDELAGVITHTGASGDDFV
ACSSS
3D structure
PDB1rds Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y37 H39 E57 D75 R76 T90 H91 F99
Catalytic site (residue number reindexed from 1) Y37 H39 E57 D75 R76 T90 H91 F99
Enzyme Commision number 4.6.1.24: ribonuclease T1.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 GPC A Y37 H39 E40 Y41 H42 D43 Y44 E45 E57 P72 G73 R76 H91 G96 D97 F99 Y37 H39 E40 Y41 H42 D43 Y44 E45 E57 P72 G73 R76 H91 G96 D97 F99
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0004540 RNA nuclease activity
GO:0016829 lyase activity
GO:0046589 ribonuclease T1 activity

View graph for
Molecular Function
External links
PDB RCSB:1rds, PDBe:1rds, PDBj:1rds
PDBsum1rds
PubMed8218254
UniProtP00653|RNMS_ASPPH Guanyl-specific ribonuclease Ms

[Back to BioLiP]