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Crystal structure of a putative 4-hydroxyproline EPIMERASE/3- hydroxyproline dehydratse from the soil bacterium ochrobacterium anthropi, target efi-506495, disordered loops

Analyse Crystal structure of a putative 4-hydroxyproline EPIMERASE/3- hydroxyproline… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K8L
Type: protein
Length: 305 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proline racemase
UniProt: A6WW16
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proline racemase	protein	305	19% helix, 41% strand	A6WW16

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	284	0.60	0.78	40	empty
2	64	0.38	0.79	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4K8L · Crystal structure of a putative 4-hydroxyproline epimerase/3-hydroxyproline dehydratse… · the same entry in another collection · chain A against A, TM-score 1.00
A6WW16 · AlphaFold monomer V2.0 prediction for 4-hydroxyproline 2-epimerase 1 (A6WW16) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 A6WW16
Elsewhere: RCSB PDB 4K8L · PDBe 4K8L · UniProt A6WW16

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