5LAB
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
Replaces: 1RMZEntity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Macrophage metalloelastase | polymer | 159 | 17615.7 | 1 | UniProt (P39900) Pfam (PF00413) | Homo sapiens (Human) | MME,Macrophage elastase,hME,Matrix metalloproteinase-12,MMP-12 |
| 2 | B, C (A) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 3 | D, E, F (A) | CALCIUM ION | non-polymer | 40.1 | 3 | Chemie (CA) | |||
| 4 | G (A) | N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID | non-polymer | 316.4 | 1 | Chemie (NGH) | |||
| 5 | H (A) | water | water | 18.0 | 236 | Chemie (HOH) |
Sequence modifications
A: 106 - 263 (UniProt: P39900)
| PDB | External Database | Details |
|---|---|---|
| Met 105 | - | initiating methionine |
| Asp 171 | Phe 171 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 17615.7 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 567.4 | |
| All* | Total formula weight | 18183.1 |
