MolNFT v1 · #113347 · protein

Y233A-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1

5ACS · Gim-1 protein: “Y233A-investigation of the impact from residues W228 and Y233 in the metallo-beta-lactamase gim-1”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.42). MolNFT v1 #113347 on GenesisL1: 3D structure…

PDB: 5ACS
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gim-1 protein
UniProt: Q704V1
Ligands: ZN
Pockets: 2 · best druggability 0.42

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gim-1 protein	protein	218	28% helix, 31% strand	Q704V1
B	Gim-1 protein	protein	217	27% helix, 31% strand	Q704V1

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	135	0.42	0.75	27	empty
2	64	0.33	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 701 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5ACS · Y233A-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 5ACS · PDBe 5ACS · UniProt Q704V1

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