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Crystal structure of E.COLI rpph-dapf in complex with GTP, MG2+ and F-

Analyse Crystal structure of E.COLI rpph-dapf in complex with GTP, MG2+ and F- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VCM
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0A6K1, P0A776
Ligands: GTP, MG, CL, F

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	275	—	P0A6K1
B	—	protein	160	—	P0A776

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains B
MG · Magnesium ion · metal · 4 copies · chains B
CL · Chloride ion · ion · chains B
F · Fluoride ion · ion · chains B

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

Compared structures

6VCM · Crystal structure of E.coli RppH-DapF in complex with GTP, Mg2+ and F- · the same entry in another collection · chain A against A, TM-score 1.00
P0A776 · AlphaFold monomer V2.0 prediction for RNA pyrophosphohydrolase (P0A776) · a predicted model of the same protein · chain B against A, TM-score 0.98
P0A6K1 · AlphaFold monomer V2.0 prediction for diaminopimelate epimerase (P0A6K1) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P0A6K1
Every structure of UniProt P0A776
Elsewhere: RCSB PDB 6VCM · PDBe 6VCM · UniProt P0A6K1 · UniProt P0A776

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