Structure of PDB 4fvl Chain A Binding Site BS01

Receptor Information

>4fvl Chain A (length=368) Species: 9606 (Homo sapiens)

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHAFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIF
KDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRK
FWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVW
RYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYS
IWSNRIVRVMPANSILWC

Ligand information

>4fvl Chain C (length=14) Species: 9606 (Homo sapiens)

QFAERYLRSYYHPT

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4fvl Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.
• Resolution: 2.436 Å
• Binding residue (original residue number in PDB): F107 P108 G183 L184 A186 H187 A188 F189 P190 P193 Y214 H222 H226 D231 P242 I243 Y244
• Binding residue (residue number reindexed from 1): F4 P5 G80 L81 A83 H84 A85 F86 P87 P90 Y111 H119 H123 D128 P139 I140 Y141

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.-

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

External links

• PDB: RCSB:4fvl, PDBe:4fvl, PDBj:4fvl
• PDBsum: 4fvl
• PubMed: 23913860
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)