1SU3: Interstitial collagenase

X-ray structure of human proMMP-1: New insights into collagenase action. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Dec 2004.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 7,098
Mol. weight: 105.24 kDa
Ligands: ZN, CA
Released: 21 Dec 2004

Explore 1SU3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SU3 contains 29 α-helices and 56 β-strands across 2 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: 14 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	33-41	9
α-helix	59-70	12
α-helix	81-87	7
β-strand	91	1	1
β-strand	113-118	6	2
α-helix	127-142	16
β-strand	148-151	4	2
β-strand	159-164	6	2
β-strand	180	1	1
β-strand	182-184	3	2
α-helix	185-186	2
β-strand	195-198	4	2
β-strand	204	1	3
β-strand	211	1	3
α-helix	212-223	12
β-strand	239	1	1
α-helix	250-260	11
α-helix	272-275	4
β-strand	286-290	5	4
β-strand	293-298	6	4
β-strand	301-304	4	4
β-strand	313-316	4	4
α-helix	317-319	3
β-strand	330-334	5	5
α-helix	335-337	3
β-strand	339-344	6	5
β-strand	347-352	6	5
β-strand	355-356	2	5
α-helix	357	1
β-strand	362-363	2	5
α-helix	364-368	5
β-strand	379-383	5	6
β-strand	388-393	6	6
β-strand	396-401	6	6
β-strand	406-407	2	6
α-helix	408	1
β-strand	413-414	2	6
α-helix	415-418	4
β-strand	428-432	5	7
β-strand	435-440	6	7
β-strand	443-448	6	7
β-strand	453-459	7	7

Chain B: 15 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	32-41	10
α-helix	59-70	12
α-helix	81-88	8
β-strand	91	1	8
β-strand	113-118	6	9
α-helix	127-142	16
β-strand	148-151	4	9
β-strand	159-164	6	9
β-strand	180	1	8
β-strand	182-184	3	9
α-helix	185-186	2
β-strand	195-198	4	9
β-strand	204	1	10
β-strand	211	1	10
α-helix	212-224	13
β-strand	239	1	8
α-helix	250-260	11
α-helix	270-272	3
β-strand	286-290	5	11
β-strand	293-298	6	11
β-strand	301-304	4	11
β-strand	313-316	4	11
α-helix	317-319	3
α-helix	325	1
β-strand	330-334	5	12
α-helix	335-337	3
β-strand	339-344	6	12
β-strand	347-352	6	12
β-strand	355-356	2	12
α-helix	357	1
β-strand	362-363	2	12
α-helix	364-368	5
β-strand	379-382	4	13
β-strand	388-393	6	13
β-strand	396-401	6	13
β-strand	406-407	2	13
α-helix	408	1
β-strand	413-414	2	13
α-helix	415-418	4
β-strand	428-432	5	14
β-strand	435-440	6	14
β-strand	443-448	6	14
β-strand	453-459	7	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interstitial collagenase	A, B	protein	450	Homo sapiens	P03956 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1SU3_1 Interstitial collagenase (chains A, B)
FPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKP
DAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQ
LWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDE
DERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAI
YGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISV
FWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDA
ALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFF
HGTRQYKFDPKTKRILTLQKANSWFNCRKN

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4
CA	Calcium ion	Ca	8

Water and common crystallization additives (EPE, SO4, NA, CL) are not listed.

Primary citation

X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding. Jozic, D., Bourenkov, G., Lim, N.H. et al. J Biol Chem (2005) 280:9578-9585. DOI 10.1074/jbc.M411084200 · 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
2TCL 2.2 Å, Structure of the catalytic domain of human fibroblast collagenase complexed with an…
3SHI 2.2 Å, Crystal structure of human MMP1 catalytic domain at 2.2 A resolution
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…

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