1GEN: C-terminal domain of gelatinase a

C-terminal domain of gelatinase a. Determined by X-ray diffraction at 2.15 Å resolution. Released 17 Aug 1996.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,677
Mol. weight: 24.82 kDa
Ligands: CA, ZN
Released: 17 Aug 1996

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

Secondary structure: helices and β-sheets

1GEN contains 8 α-helices and 18 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: 8 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	473-475	3
β-strand	477-481	5	1
β-strand	484-489	6	1
β-strand	492-496	5	1
α-helix	502-503	2
β-strand	504-508	5	1
α-helix	509-511	3
β-strand	522-526	5	2
β-strand	531-536	6	2
β-strand	539-544	6	2
β-strand	547-548	2	2
β-strand	554-555	2	2
α-helix	556-559	4
β-strand	570-574	5	3
β-strand	579-584	6	3
β-strand	587-592	6	3
β-strand	597-598	2	3
α-helix	599	1
β-strand	604-605	2	3
α-helix	606-609	4
α-helix	613-614	2
β-strand	619-622	4	4
β-strand	628-633	6	4
β-strand	636-641	6	4
β-strand	644-652	9	4
α-helix	653-656	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Gelatinase a	A	protein	218	Homo sapiens	P08253 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GEN_1 GELATINASE A (chains A)
ELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDK
PMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLP
PDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVD
LQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
ZN	Zinc ion	Zn	1

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

Primary citation

Crystal structure of the haemopexin-like C-terminal domain of gelatinase A. Libson, A.M., Gittis, A.G., Collier, I.E. et al. Nat Struct Biol (1995) 2:938-942. DOI 10.1038/nsb1195-938 · 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
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
1CK7 2.8 Å, Gelatinase a (full-length)
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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