3SHI: Human MMP1 catalytic domain

Crystal structure of human MMP1 catalytic domain at 2.2 A resolution. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Sept 2011.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,024
Mol. weight: 53.13 kDa
Ligands: CA, ZN
Released: 21 Sept 2011

Explore 3SHI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3SHI contains 12 α-helices and 21 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	113-118	6	1
α-helix	127-142	16
β-strand	148-151	4	1
β-strand	159-164	6	1
β-strand	182-184	3	1
β-strand	195-198	4	1
β-strand	204	1	2
β-strand	211	1	2
α-helix	212-223	12
α-helix	250-260	11

Chain G: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	113-118	6	3
α-helix	127-142	16
β-strand	148-151	4	3
β-strand	159-164	6	3
β-strand	182-184	3	3
α-helix	185-186	2
β-strand	195-198	4	3
β-strand	204	1	4
β-strand	211	1	4
α-helix	212-224	13
α-helix	250-260	11

Chain M: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	113-118	6	5
α-helix	127-142	16
β-strand	148-151	4	5
β-strand	159-164	6	5
β-strand	182-184	3	5
α-helix	185-186	2
β-strand	195-198	4	5
α-helix	202-203	2
β-strand	204	1	6
β-strand	211	1	6
α-helix	212-224	13
α-helix	250-260	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interstitial collagenase	A, G, M	protein	156	Homo sapiens	P03956 (AlphaFold model)

Sequence of entity 1 (A, G, M), FASTA

>3SHI_1 Interstitial collagenase (chains A, G, M)
NPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVR
GDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLG
LSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYG

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	9
ZN	Zinc ion	Zn	6

Primary citation

The catalytic domain of MMP-1 studied through tagged lanthanides. Bertini, I., Calderone, V., Cerofolini, L. et al. FEBS Lett (2012) 586:557-567. DOI 10.1016/j.febslet.2011.09.020 · PubMed

Other PDB entries of the same protein (UniProt P03956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1HFC 1.5 Å, 1.56 Å structure of mature truncated human fibroblast collagenase
1CGE 1.9 Å, Crystal structures of recombinant 19-kda human fibroblast collagenase complexed to itself
966C 1.9 Å, Crystal structure of fibroblast collagenase-1 complexed to a diphenyl-ether sulphone…
1CGF 2.1 Å, Crystal structures of recombinant 19-kda human fibroblast collagenase complexed to itself
1SU3 2.2 Å, X-ray structure of human proMMP-1: New insights into collagenase action
2TCL 2.2 Å, Structure of the catalytic domain of human fibroblast collagenase complexed with an…
1CGL 2.4 Å, Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
2J0T 2.54 Å, Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain…
2CLT 2.67 Å, Crystal structure of the active form (full-length) of human fibroblast collagenase.
4AUO 3.0 Å, Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide
1AYK Inhibitor-free catalytic fragment of human fibroblast collagenase, NMR, 30 structures
2AYK Inhibitor-free catalytic fragment of human fibroblast collagenase, NMR, minimized…

Browse structure collections

About this viewer

MolViewer shows 3SHI directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.