Structure of PDB 4g0d Chain C

Receptor sequence
>4g0dC (length=368) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHAFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIF
KDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRK
FWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVW
RYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYS
IWSNRIVRVMPANSILWC
3D structure
PDB4g0d Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.
ChainC
Resolution2.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H222 A223 H226 H232
Catalytic site (residue number reindexed from 1) H119 A120 H123 H129
Enzyme Commision number 3.4.24.-
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4g0d, PDBe:4g0d, PDBj:4g0d
PDBsum4g0d
PubMed23913860
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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