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3BA0

Crystal structure of full-length human MMP-12

Summary for 3BA0
Entry DOI10.2210/pdb3ba0/pdb
Related1SU3
DescriptorMacrophage metalloelastase, ZINC ION, CALCIUM ION, ... (5 entities in total)
Functional Keywordsfull-length mmp-12, hemopexin domain, catalytic domain, domain interaction., calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight42509.54
Authors
Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Myonas, E.,Svergun, D.I. (deposition date: 2007-11-07, release date: 2008-07-29, Last modification date: 2023-11-01)
Primary citationBertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Mylonas, E.,Svergun, D.I.
Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12.
J.Am.Chem.Soc., 130:7011-7021, 2008
Cited by
PubMed: 18465858
DOI: 10.1021/ja710491y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

218853

数据于2024-04-24公开中

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