9ASX: Cathepsin-G

BIFUNCTIONAL INHIBITION OF NEUTROPHIL ELASTASE AND CATHEPSIN G by Eap3 of S. aureus. Determined by X-ray diffraction at 1.96 Å resolution. Released 12 Jun 2024.

Method: X-ray diffraction
Resolution: 1.96 Å
Organisms: Homo sapiens, Staphylococcus aureus subsp. aureus Mu50
Chains: 3
Atoms: 4,519
Mol. weight: 61.69 kDa
Ligands: NAG
Released: 12 Jun 2024

Explore 9ASX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ASX contains 21 α-helices and 51 β-strands across 3 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, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-36	7	3
β-strand	41-50	10	3
β-strand	53-56	4	3
α-helix	58-60	3
β-strand	64-69	6	3
β-strand	73	1	4
β-strand	82-91	10	3
β-strand	96	1	5
β-strand	101	1	5
β-strand	105-109	5	3
β-strand	123	1	2
β-strand	136-141	6	2
β-strand	153	1	4
β-strand	155-161	7	2
α-helix	162-163	2
α-helix	164-168	5
β-strand	179-182	4	2
β-strand	190	1	1
α-helix	198	1
β-strand	199-202	4	2
β-strand	205-213	9	2
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	2
α-helix	226-229	4
α-helix	230-237	8

Chain B: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	6
β-strand	33-34	2	7
α-helix	35-36	2
β-strand	43-48	6	8
β-strand	51-60	10	8
β-strand	63-66	4	8
α-helix	68-71	4
α-helix	76-78	3
β-strand	80-83	4	8
β-strand	87	1	9
β-strand	96-105	10	8
β-strand	109	1	10
β-strand	114	1	10
β-strand	118-122	5	8
α-helix	126-128	3
α-helix	134-139	6
α-helix	144-145	2
β-strand	149-154	6	7
β-strand	157	1	11
β-strand	164	1	11
β-strand	167	1	9
β-strand	169-176	8	7
β-strand	185-188	4	7
β-strand	195	1	6
β-strand	204-207	4	7
β-strand	210-219	10	7
α-helix	228	1
β-strand	229-233	5	7
α-helix	234-237	4
α-helix	238-245	8

Chain C: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	267-275	9	3
β-strand	278	1	3
β-strand	279-280	2	2
β-strand	283-289	7	3
β-strand	293-294	2	12
α-helix	296-311	16
α-helix	315-319	5
β-strand	324-330	7	3
β-strand	335-339	5	3
β-strand	344-346	3	7
β-strand	350-351	2	12
α-helix	352-354	3
β-strand	355-362	8	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cathepsin-G	A	protein	223	Homo sapiens	P08311 (AlphaFold model)
Neutrophil elastase	B	protein	218	Homo sapiens	P08246 (AlphaFold model)
Extracellular Adherence Protein	C	protein	100	Staphylococcus aureus subsp. aureus Mu50	Q99QS1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9ASX_1 Cathepsin-G (chains A)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR

Sequence of entity 2 (B), FASTA

>9ASX_2 Neutrophil elastase (chains B)
IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNL
SRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGV
QCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCN
GLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ

Sequence of entity 3 (C), FASTA

>9ASX_3 Extracellular Adherence Protein (chains C)
GSTYQVPYSINLNGTSTNILSNLSFSNKPWTNYKNLTSQIKSVLKHDRGISEQDLKYAKK
AYYTVYFKNGGKRILQLNSKNYTANLVHAKDVKRIEITVK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. Mishra, N., Gido, C.D., Herdendorf, T.J. et al. J Biol Chem (2024) 300:107627-107627. DOI 10.1016/j.jbc.2024.107627 · 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
9ATK 2.11 Å, BIFUNCTIONAL INHIBITION OF NEUTROPHIL ELASTASE AND CATHEPSIN G by Eap4 of S. aureus

Browse structure collections

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