MolNFT v1 · #61216 · protein

Crystal structure of SH1221 protein from staphylococcus haemolyticus, northeast structural genomics consortium target SHR87

3DEV: “Crystal structure of SH1221 protein from staphylococcus haemolyticus, northeast structural genomics…”. X-ray diffraction, 2 ligands (MG, SO4), 2 pockets (best druggability 0.67). MolNFT v1 #61216 on GenesisL1: 3D structure, binding…

PDB: 3DEV
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SH1221
UniProt: Q4L745
Ligands: MG, SO4
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	SH1221	protein	316	40% helix, 18% strand	Q4L745

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 3 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	867	0.67	0.74	75	SO4
2	50	0.20	0.71	10	empty

Interfaces

1 interface between chains.

A–B · 1673 Å² buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3DEV · Crystal structure of SH1221 protein from Staphylococcus haemolyticus, Northeast… · 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 Q4L745
Elsewhere: RCSB PDB 3DEV · PDBe 3DEV · UniProt Q4L745

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