P08253: 72 kDa type IV collagenase (MMP2)

72 kDa type IV collagenase (MMP2) is a 660-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08253.

Gene
MMP2
Organism
Homo sapiens
Length
660 residues
Mean pLDDT
89.8
Model
AF-P08253-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate77%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14

Subunit structure

Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B

Subcellular location

Secreted, extracellular space, extracellular matrix, Membrane, Nucleus, Cytoplasm, Mitochondrion

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3AYUX-ray2.0 ÅA=110-450
7XJOX-ray2.0 ÅA/B=110-450
1GENX-ray2.15 ÅA=443-660
8H78X-ray2.4 ÅA/B=110-450
1RTGX-ray2.6 ÅA=451-660
1EAKX-ray2.66 ÅA/B/C/D=32-452
1CK7X-ray2.8 ÅA=30-660
1QIBX-ray2.8 ÅA=115-213, A=394-449
7XGJX-ray2.8 ÅA/B/C=110-450
1GXDX-ray3.1 ÅA/B=30-660
1CXWNMRA=278-336
1HOVNMRA=110-214
1J7MNMRA=337-394
1KS0NMRA=223-282

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