4AUO: MMP-1(E200A)

Crystal structure of MMP-1(E200A) in complex with a triple-helical collagen peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 11 Jul 2012.

Method: X-ray diffraction
Resolution: 3.0 Å
Organisms: HOMO SAPIENS, SYNTHETIC CONSTRUCT
Chains: 8
Atoms: 7,387
Mol. weight: 107.74 kDa
Ligands: CA, ZN
Released: 11 Jul 2012

Explore 4AUO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AUO contains 38 α-helices and 57 β-strands across 8 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: 12 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	82-83	2	1
β-strand	94-98	5	2
α-helix	108-123	16
β-strand	129-132	4	2
β-strand	140-141	2	2
β-strand	142-145	4	3
β-strand	163-165	3	3
β-strand	176-179	4	3
β-strand	185	1	4
β-strand	192	1	4
α-helix	193-205	13
β-strand	207-208	2	1
α-helix	231-240	10
α-helix	253-256	4
β-strand	267-269	3	5
α-helix	271-273	3
β-strand	275-279	5	5
β-strand	282-286	5	5
β-strand	294-297	4	5
α-helix	298-300	3
α-helix	306	1
β-strand	311-315	5	6
α-helix	316-318	3
β-strand	320-325	6	6
β-strand	328-333	6	6
β-strand	336-337	2	6
α-helix	338	1
β-strand	343-344	2	6
α-helix	345-349	5
β-strand	360-363	4	7
β-strand	369-374	6	7
β-strand	377-382	6	7
β-strand	387-388	2	7
β-strand	394-395	2	7
α-helix	396-399	4
β-strand	409-413	5	8
β-strand	416-421	6	8
β-strand	424-429	6	8
β-strand	434-440	7	8
α-helix	441-444	4

Chain B: 11 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	82-83	2	9
α-helix	84	1
β-strand	94-99	6	10
α-helix	108-123	16
β-strand	129-132	4	10
β-strand	140-145	6	10
β-strand	163-165	3	10
β-strand	176-179	4	10
β-strand	185	1	11
β-strand	192	1	11
α-helix	193-203	11
β-strand	207-208	2	9
α-helix	231-240	10
α-helix	253-256	4
β-strand	267-269	3	12
β-strand	275-279	5	12
β-strand	282-286	5	12
β-strand	294-297	4	12
α-helix	298-300	3
α-helix	306	1
β-strand	311-315	5	13
α-helix	316-318	3
β-strand	320-325	6	13
β-strand	328-333	6	13
β-strand	336-337	2	13
α-helix	338	1
β-strand	343-344	2	13
α-helix	345-348	4
β-strand	360-363	4	14
β-strand	369-374	6	14
β-strand	377-382	6	14
β-strand	387-388	2	14
β-strand	394-395	2	14
α-helix	396-399	4
β-strand	409-413	5	15
β-strand	416-421	6	15
β-strand	424-429	6	15
β-strand	434-440	7	15

Chain C: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	964-966	3
α-helix	973-980	8
α-helix	984-994	11

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	971-979	9
α-helix	981-992	12

Chain E: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	970-979	10
α-helix	981-985	5
α-helix	988-992	5

Chain F: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	964-968	5
α-helix	976-979	4
β-strand	983	1	16
α-helix	984-991	8

Chain G: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	970-973	4
α-helix	975-980	6
β-strand	982	1	16
α-helix	992-997	6

Chain H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	970-983	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interstitial collagenase	A, B	protein	367	HOMO SAPIENS	P03956 (AlphaFold model)
Triple-helical collagen peptide	C, D, E, F, G, H	protein	40	SYNTHETIC CONSTRUCT

Sequence of entity 1 (A, B), FASTA

>4AUO_1 INTERSTITIAL COLLAGENASE (chains A, B)
FVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADI
MISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHA
LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACD
SKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDE
VRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWR
YDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQK
ANSWFNC

Sequence of entity 2 (C, D, E, F, G, H), FASTA

>4AUO_2 TRIPLE-HELICAL COLLAGEN PEPTIDE (chains C, D, E, F, G, H)
GPPGPPGPPGPQGLAGQRGIVGLPGQRGERGPPGPPGPPG

Ligands and cofactors

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

Primary citation

Structural Insights Into Triple-Helical Collagen Cleavage by Matrix Metalloproteinase 1. Manka, S.W., Carafoli, F., Visse, R. et al. Proc Natl Acad Sci U S A (2012) 109:12461. DOI 10.1073/PNAS.1204991109 · 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…
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.
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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