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C-terminal domain of gelatinase a

Analyse C-terminal domain of gelatinase a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GEN
Type: protein
Length: 200 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gelatinase a
EC: 3.4.24.24
UniProt: P08253
Ligands: ZN, CA, NA, CL
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gelatinase a (EC 3.4.24.24)	protein	200	8% helix, 44% strand	P08253

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CA · Calcium ion · metal · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.46	0.81	22	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1GEN · C-terminal domain of gelatinase a · the same entry in another collection · chain A against A, TM-score 1.00
P08253 · AlphaFold monomer V2.0 prediction for 72 kda type IV collagenase (P08253) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P08253
Elsewhere: RCSB PDB 1GEN · PDBe 1GEN · UniProt P08253

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