MolNFT v1 · #61714 · protein

Crystal structure of the metal-dependent hd domain- containing hydrolase BH2835 from bacillus halodurans, northeast structural genomics consortium target BHR130.

3DTO · BH2835 protein: “Crystal structure of the metal-dependent hd domain- containing hydrolase BH2835 from bacillus halodurans…”. X-ray diffraction, 12 pockets (best druggability 0.68). MolNFT v1 #61714 on GenesisL1: 3D structure…

PDB: 3DTO
Type: protein
Length: 756 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BH2835 protein
UniProt: Q9K916
Pockets: 12 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	BH2835 protein	protein	189	69% helix, 0% strand	Q9K916

Pockets

12 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	811	0.68	0.75	68	empty
2	266	0.52	0.75	42	empty
3	107	0.45	0.79	21	empty
4	138	0.43	0.76	26	empty
5	145	0.43	0.75	26	empty

Interfaces

3 interfaces between chains.

A–B · 1223 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 1213 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 284 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

3DTO · Crystal structure of the metal-dependent HD domain-containing hydrolase BH2835 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 Q9K916
Elsewhere: RCSB PDB 3DTO · PDBe 3DTO · UniProt Q9K916

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