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Structures of RNase a complexed with 3'-cmp and D(CPA): active site conformation and conserved water molecules

Analyse Structures of RNase a complexed with 3'-cmp and D(CPA): active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RPG
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease a
EC: 3.1.27.5
UniProt: P61823
Ligands: CPA
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease a (EC 3.1.27.5)	protein	124	21% helix, 35% strand	P61823

Ligands and binding sites

CPA · 2'-deoxycytidine-2'-deoxyadenosine-3',5'-monophosphate · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.27	0.73	18	CPA

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1RPG · Structures of RNase a complexed with 3'-cmp and D(CPA): active site conformation and… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P61823
Elsewhere: RCSB PDB 1RPG · PDBe 1RPG · UniProt P61823

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