MolNFT v1 · #57075 · protein

Crystal structure of TTHA1623 in a di-iron-bound form

2ZZI · Metallo-beta-lactamase superfamily protein: “Crystal structure of TTHA1623 in a di-iron-bound form”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.72). MolNFT v1 #57075 on GenesisL1: 3D structure, binding sites…

PDB: 2ZZI
Type: protein
Length: 397 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo-beta-lactamase superfamily protein
UniProt: Q5SHV7
Ligands: FE
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo-beta-lactamase superfamily protein	protein	198	28% helix, 26% strand	Q5SHV7
B	Metallo-beta-lactamase superfamily protein	protein	199	28% helix, 26% strand	Q5SHV7

Ligands and binding sites

FE · Fe (III) ion · metal · 4 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	562	0.72	0.80	55	empty
2	124	0.46	0.78	19	ACT
3	120	0.44	0.77	21	ACT

Interfaces

1 interface between chains.

A–B · 437 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2ZZI · Crystal structure of TTHA1623 in a di-iron-bound form · 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 Q5SHV7
Elsewhere: RCSB PDB 2ZZI · PDBe 2ZZI · UniProt Q5SHV7

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