1CK7: Gelatinase a

Gelatinase a (full-length). Determined by X-ray diffraction at 2.8 Å resolution. Released 25 Aug 1999.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,051
Mol. weight: 71.5 kDa
Ligands: CA, ZN
Released: 25 Aug 1999

Explore 1CK7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CK7 contains 24 α-helices and 54 β-strands across 1 chain. 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: 24 helices, 54 β-strands

Element	Residues	Length	Sheet
α-helix	36-37	2
α-helix	42-45	4
α-helix	46-57	12
α-helix	67-81	15
α-helix	91-96	6
β-strand	101	1	1
β-strand	123-128	6	2
α-helix	137-152	16
β-strand	158-161	4	2
β-strand	169-174	6	2
β-strand	190	1	1
β-strand	192-194	3	2
α-helix	195-196	2
β-strand	205-208	4	2
β-strand	213-214	2	3
β-strand	222	1	4
β-strand	232	1	4
α-helix	233	1
β-strand	237-239	3	5
β-strand	242-244	3	5
β-strand	248	1	6
β-strand	258-260	3	6
β-strand	264	1	5
α-helix	265-268	4
β-strand	271-273	3	6
α-helix	274-275	2
β-strand	282	1	7
α-helix	289-291	3
β-strand	295-296	2	8
β-strand	301-302	2	8
β-strand	306	1	7
β-strand	316-318	3	7
β-strand	322	1	8
α-helix	323-326	4
β-strand	329-331	3	7
β-strand	340	1	9
α-helix	347-349	3
β-strand	353-355	3	10
β-strand	358-360	3	10
β-strand	364	1	9
β-strand	374-376	3	9
β-strand	380	1	10
α-helix	381-384	4
β-strand	387-389	3	9
α-helix	390-391	2
β-strand	395-396	2	3
α-helix	397-409	13
β-strand	424	1	1
α-helix	435-444	10
β-strand	477-480	4	11
β-strand	485-488	4	11
β-strand	492-496	5	11
α-helix	502-503	2
β-strand	504-508	5	11
α-helix	509-511	3
β-strand	522	1	12
β-strand	525-526	2	12
β-strand	531-536	6	12
β-strand	539-544	6	12
β-strand	547-548	2	12
α-helix	549	1
β-strand	554-555	2	12
α-helix	556-559	4
β-strand	570	1	13
β-strand	579-584	6	13
β-strand	587-592	6	13
β-strand	597-598	2	13
α-helix	599	1
β-strand	604-605	2	13
α-helix	613-614	2
β-strand	619-621	3	14
β-strand	628	1	15
β-strand	630-633	4	14
β-strand	636-638	3	14
β-strand	641	1	15
β-strand	644	1	15
β-strand	650	1	14
α-helix	653-657	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (gelatinase a)	A	protein	631	Homo sapiens	P08253 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CK7_1 PROTEIN (GELATINASE A) (chains A)
APSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDL
DQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQ
VWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDD
DELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDG
KYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKY
GFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGF
CPDQGYSLFLVAAHAFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASP
DIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLV
ATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVD
AAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHS
YFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	3
ZN	Zinc ion	Zn	2

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

Primary citation

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Morgunova, E., Tuuttila, A., Bergmann, U. et al. Science (1999) 284:1667-1670. DOI 10.1126/science.284.5420.1667 · PubMed

Other PDB entries of the same protein (UniProt P08253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3AYU 2.0 Å, Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide…
7XJO 2.0 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1GEN 2.15 Å, C-terminal domain of gelatinase a
8H78 2.4 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1RTG 2.6 Å, C-terminal domain (haemopexin-like domain) of human matrix metalloproteinase-2
1EAK 2.66 Å, Catalytic domain of proMMP-2 E404Q mutant
1QIB 2.8 Å, Crystal structure of gelatinase a catalytic domain
7XGJ 2.8 Å, Crystal structure of human MMP-2 catalytic domain in complex with inhibitor
1GXD 3.1 Å, proMMP-2/TIMP-2 complex
1CXW The second type II module from human matrix metalloproteinase 2
1HOV Solution structure of a catalytic domain of mmp-2 complexed with sc-74020
1J7M The Third Fibronectin Type II Module from Human Matrix Metalloproteinase 2

Browse structure collections

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