MolNFT v1 · #139254 · protein

Crystal structure of hasap with fe-5,15-diazaporphyrin

5XA4 · Heme acquisition protein hasap: “Crystal structure of hasap with fe-5,15-diazaporphyrin”. X-ray diffraction, 1 ligand (83L), 4 pockets (best druggability 0.75). MolNFT v1 #139254 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5XA4
Type: protein
Length: 368 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme acquisition protein hasap
UniProt: G3XD33
Ligands: 83L
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Heme acquisition protein hasap	protein	184	32% helix, 36% strand	G3XD33

Ligands and binding sites

83L · 10,20-Diphenyl-5,15-diaza-porphyrin containing FE · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.75	0.94	28	empty
2	253	0.65	0.82	36	83L
3	146	0.52	0.79	23	83L
4	75	0.34	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 795 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5XA4 · Crystal Structure of HasAp with Fe-5,15-Diazaporphyrin · 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 G3XD33
Elsewhere: RCSB PDB 5XA4 · PDBe 5XA4 · UniProt G3XD33

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