1KYN: Cathepsin-G

Cathepsin-G. Determined by X-ray diffraction at 3.5 Å resolution. Released 1 May 2002.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,607
Mol. weight: 54.36 kDa
Ligands: KTP
Released: 1 May 2002

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

Secondary structure: helices and β-sheets

1KYN contains 16 α-helices and 46 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: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30	1	3
β-strand	32	1	4
β-strand	33	1	5
β-strand	42	1	5
β-strand	45-46	2	3
β-strand	51-54	4	3
β-strand	65-68	4	4
β-strand	72	1	6
β-strand	81-84	4	4
β-strand	85-90	6	3
β-strand	104-108	5	3
β-strand	115	1	7
β-strand	118	1	7
α-helix	122-125	4
β-strand	135-140	6	2
β-strand	154	1	6
β-strand	156-161	6	2
α-helix	162-164	3
α-helix	165-169	5
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-200	3	2
β-strand	209-216	8	2
α-helix	221	1
α-helix	225	1
β-strand	226-230	5	2
α-helix	231-233	3
α-helix	235-242	8

Chain B: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	317	1	8
β-strand	320-321	2	9
α-helix	322-323	2
β-strand	330	1	10
β-strand	332	1	11
β-strand	333	1	12
β-strand	342	1	12
β-strand	345-346	2	10
β-strand	351-354	4	10
β-strand	365-368	4	11
β-strand	372	1	13
β-strand	381-384	4	11
β-strand	385-390	6	10
β-strand	404-408	5	10
β-strand	415	1	14
β-strand	418	1	14
α-helix	422-425	4
β-strand	435-440	6	9
β-strand	454	1	13
β-strand	456-461	6	9
α-helix	462-464	3
α-helix	465-469	5
β-strand	480-483	4	9
β-strand	489	1	8
β-strand	498-500	3	9
β-strand	509-516	8	9
α-helix	521	1
α-helix	525	1
β-strand	526-530	5	9
α-helix	531-533	3
α-helix	535-542	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cathepsin G	A, B	protein	235	Homo sapiens	P08311 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1KYN_1 cathepsin G (chains A, B)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL

Ligands and cofactors

ID	Name	Formula	Copies
KTP	(2-naphthalen-2-yl-1-naphthalen-1-yl-2-oxo-ethyl)-phosphonic acid	C22 H17 O4 P	2

Primary citation

Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design. Greco, M.N., Hawkins, M.J., Powell, E.T. et al. J Am Chem Soc (2002) 124:3810-3811. DOI 10.1021/ja017506h · PubMed

Other PDB entries of the same protein (UniProt P08311 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7H6G 1.21 Å, THE 1.21 A CRYSTAL STRUCTURE OF HUMAN CATHEPSIN G IN COMPLEX WITH…
6VTM 1.6 Å, Human Cathepsin-G Inhibited by S. aureus EapH1
1CGH 1.8 Å, Human cathepsin G
8G25 1.8 Å, Crystal Structure of Cathepsin-G and Neutrophil Elastase Inhibited by S. aureus EapH2 at…
8G24 1.82 Å, Crystal Structure of Cathepsin-G and Neutrophil Elastase Inhibited by S. aureus EapH2 at…
1T32 1.85 Å, A Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase with Therapeutic…
8D4V 1.85 Å, Crystal Structure of Cathepsin G Inhibited by Eap2 from S. aureus
8G26 1.85 Å, Crystal Structure of Cathepsin-G and Neutrophil Elastase Inhibited by S. aureus EapH2 at…
1AU8 1.9 Å, Human cathepsin G
7H6H 1.94 Å, THE 1.94 A CRYSTAL STRUCTURE OF HUMAN CATHEPSIN G IN COMPLEX WITH…
8D4S 1.95 Å, Crystal Structure of Cathepsin G Inhibited by Eap1 from S. aureus
9ASX 1.96 Å, BIFUNCTIONAL INHIBITION OF NEUTROPHIL ELASTASE AND CATHEPSIN G by Eap3 of S. aureus

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