7H6G: Cathepsin G

THE 1.21 A CRYSTAL STRUCTURE OF HUMAN CATHEPSIN G IN COMPLEX WITH N-[2-[6-fluoro-2-[(4-hydroxy-5-methyl-2-oxo-5-phenylfuran-3-yl)-phenylmethyl]-1H-indol-3-yl]ethyl]acetamide. Determined by X-ray diffraction at 1.21 Å resolution. Released 5 Mar 2025.

Method: X-ray diffraction
Resolution: 1.21 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,438
Mol. weight: 55.46 kDa
Ligands: ZN, A1AOS, BTB
Released: 5 Mar 2025

Explore 7H6G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7H6G contains 19 α-helices and 43 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: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-36A	8	3
β-strand	38-48	11	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	63-68	6	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	104-108	5	3
β-strand	115	1	5
β-strand	118	1	5
α-helix	124-125	2
β-strand	135-140	6	2
β-strand	145	1	6
β-strand	148	1	6
β-strand	154	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-169	5
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-215	8	2
α-helix	221	1
α-helix	225	1
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-244	10

Chain B: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	7
β-strand	20-21	2	8
α-helix	22-23	2
β-strand	30-36A	8	9
β-strand	38-48	11	9
β-strand	51-54	4	9
α-helix	56-58	3
β-strand	63-68	6	9
β-strand	72	1	10
β-strand	81-90	10	9
β-strand	95	1	11
β-strand	100	1	11
β-strand	104-108	5	9
α-helix	111-114	4
β-strand	115	1	12
β-strand	118	1	12
β-strand	122	1	8
α-helix	124-125	2
β-strand	135-140	6	8
β-strand	154	1	10
β-strand	156-162	7	8
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	8
β-strand	189	1	7
β-strand	198-201	4	8
β-strand	204-215	8	8
α-helix	221	1
α-helix	225	1
β-strand	226-230	5	8
α-helix	231-233	3
α-helix	235-243	9

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

>7H6G_1 Cathepsin G (chains A, B)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4
A1AOS	N-(2-{6-fluoro-2-[(R)-[(5R)-4-hydroxy-5-methyl-2-oxo-5-phenyl-2,5-dihydrofuran-…	C30 H27 F N2 O4	2
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	1

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

Primary citation

The CASP 16 Experimental Protein-Ligand Datasets. Tosstorff, A., Rudolph, M.G., Benz, J. et al. Proteins (2026) 94:79-85. DOI 10.1002/prot.70053 · PubMed

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

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
9ATK 2.11 Å, BIFUNCTIONAL INHIBITION OF NEUTROPHIL ELASTASE AND CATHEPSIN G by Eap4 of S. aureus

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