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The crystal structure of human emmprin N-terminal domain 1 in P6(1)22 space group

Analyse The crystal structure of human emmprin N-terminal domain 1 in P6(1)22 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I84
Type: protein
Length: 164 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cervical emmprin
UniProt: Q54A51
Ligands: CL
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cervical emmprin	protein	79	4% helix, 66% strand	Q54A51
B	Cervical emmprin	protein	85	0% helix, 59% strand	Q54A51

Ligands and binding sites

CL · Chloride ion · ion · chains 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.43	0.80	17	empty
2	57	0.36	0.79	21	empty

Interfaces

1 interface between chains.

A–B · 1571 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3I84 · The Crystal Structure of Human EMMPRIN N-terminal Domain 1 in P6(1)22 space group · 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 Q54A51
Elsewhere: RCSB PDB 3I84 · PDBe 3I84 · UniProt Q54A51

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