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Apo structure of tp domain from chlamydia trachomatis penicillin- binding protein 3

Analyse Apo structure of tp domain from chlamydia trachomatis penicillin- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HZH
Type: protein
Length: 672 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Penicillin-binding protein
EC: 2.4.1.129
UniProt: A0A0E9FXJ8
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Penicillin-binding protein (EC 2.4.1.129)	protein	330	35% helix, 21% strand	A0A0E9FXJ8
B	Penicillin-binding protein (EC 2.4.1.129)	protein	342	34% helix, 23% strand	A0A0E9FXJ8

Pockets

5 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	549	0.69	0.79	58	empty
2	144	0.62	0.85	31	empty
3	114	0.42	0.76	17	empty
4	53	0.29	0.75	11	empty
5	57	0.28	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 772 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6HZH · Apo structure of TP domain from Chlamydia trachomatis penicillin-binding protein 3 · 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 A0A0E9FXJ8
Elsewhere: RCSB PDB 6HZH · PDBe 6HZH · UniProt A0A0E9FXJ8

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