MolNFT v1 · #113348 · protein

W228S-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1

5ACT · Gim-1 protein: “W228S-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.56). MolNFT v1 #113348 on GenesisL1: 3D structure…

PDB: 5ACT
Type: protein
Length: 437 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gim-1 protein
UniProt: Q704V1
Ligands: ZN
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gim-1 protein	protein	219	27% helix, 31% strand	Q704V1
B	Gim-1 protein	protein	218	27% helix, 31% strand	Q704V1

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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	325	0.56	0.75	45	empty

Interfaces

1 interface between chains.

A–B · 775 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

5ACT · W228S-Investigation of the impact from residues W228 and Y233 in the… · 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 Q704V1
Elsewhere: RCSB PDB 5ACT · PDBe 5ACT · UniProt Q704V1

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