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Structure of yeast POLY(A) polymerase in a closed conformation.

Analyse Structure of yeast POLY(A) polymerase in a closed conformation. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HHP
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(A) polymerase
EC: 2.7.7.19
UniProt: P29468
Ligands: MG
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	POLY(A) polymerase (EC 2.7.7.19)	protein	508	45% helix, 17% strand	P29468

Ligands and binding sites

MG · Magnesium ion · metal · chains A
FLC · Citrate anion · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	782	0.70	0.76	57	FLC, MG

Compared structures

2HHP · Structure of yeast poly(A) polymerase in a closed conformation. · the same entry in another collection · chain A against A, TM-score 1.00
P29468 · AlphaFold monomer V2.0 prediction for POLY(A) polymerase (P29468) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P29468
Elsewhere: RCSB PDB 2HHP · PDBe 2HHP · UniProt P29468

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