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Structure of dimeric holo hasap H32A mutant from pseudomonas aeruginosa to 1.20A resolution

Analyse Structure of dimeric holo hasap H32A mutant from pseudomonas aeruginosa to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MOL
Type: protein
Length: 357 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme acquisition protein hasap
UniProt: Q02QP5
Ligands: HEM
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme acquisition protein hasap	protein	183	32% helix, 36% strand	Q02QP5
B	Heme acquisition protein hasap	protein	174	32% helix, 36% strand	Q02QP5

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	641	0.74	0.80	50	HEM
2	83	0.45	0.80	23	empty

Interfaces

1 interface between chains.

A–B · 528 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3MOL · Structure of dimeric holo HasAp H32A Mutant from Pseudomonas aeruginosa to 1.20A… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q02QP5
Elsewhere: RCSB PDB 3MOL · PDBe 3MOL · UniProt Q02QP5

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