MolNFT v1 · #181332 · protein

Structure of the siderophore interacting protein from acinetbacter baumannii

7LRN · NADPH-dependent ferric siderophore reductase: “Structure of the siderophore interacting protein from acinetbacter baumannii”. X-ray diffraction, 1 ligand (FAD), 2 pockets (best druggability 0.79). MolNFT v1 #181332 on GenesisL1: 3D…

PDB: 7LRN
Type: protein
Length: 496 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADPH-dependent ferric siderophore reductase
UniProt: A0A1E3M8P2
Ligands: FAD
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADPH-dependent ferric siderophore reductase	protein	246	27% helix, 38% strand	A0A1E3M8P2
B	NADPH-dependent ferric siderophore reductase	protein	250	27% helix, 37% strand	A0A1E3M8P2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	937	0.79	0.81	108	FAD
2	489	0.72	0.82	53	FAD

Interfaces

1 interface between chains.

A–B · 898 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

7LRN · Structure of the Siderophore Interacting Protein from Acinetbacter baumannii · 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 A0A1E3M8P2
Elsewhere: RCSB PDB 7LRN · PDBe 7LRN · UniProt A0A1E3M8P2

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