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A pH-dependent stablization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase

Analyse A pH-dependent stablization of an active site loop observed from low and high… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GAR
Type: protein
Length: 188 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycinamide ribonucleotide transformylase
EC: 2.1.2.2
UniProt: P08179
Ligands: PO4
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycinamide ribonucleotide transformylase (EC 2.1.2.2)	protein	188	35% helix, 26% strand	P08179

Ligands and binding sites

PO4 · Phosphate ion · ion · 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	102	0.35	0.74	22	PO4

Compared structures

2GAR · A pH-dependent stablization of an active site loop observed from low and high pH crystal… · the same entry in another collection · chain A against A, TM-score 1.00
P08179 · AlphaFold monomer V2.0 prediction for phosphoribosylglycinamide formyltransferase (P08179) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P08179
Elsewhere: RCSB PDB 2GAR · PDBe 2GAR · UniProt P08179

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