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Crystal structure of hypd, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase from sinorhizobium meliloti

Analyse Crystal structure of hypd, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CZJ
Type: protein
Length: 637 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthase
EC: 3.5.4.22
UniProt: Q92WT0
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrodipicolinate synthase (EC 3.5.4.22)	protein	318	53% helix, 12% strand	Q92WT0
B	Dihydrodipicolinate synthase (EC 3.5.4.22)	protein	319	54% helix, 12% strand	Q92WT0

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	721	0.83	0.86	95	empty
2	150	0.49	0.78	32	empty

Interfaces

1 interface between chains.

A–B · 1072 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5CZJ · Crystal structure of HypD, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase from… · 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 Q92WT0
Elsewhere: RCSB PDB 5CZJ · PDBe 5CZJ · UniProt Q92WT0

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