8D7K: Cathepsin G, C-terminal truncated form

Bifunctional Inhibition of Neutrophil Elastase and Cathepsin G by Eap2 from S. aureus. Determined by X-ray diffraction at 3.1 Å resolution. Released 14 Jun 2023.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: Homo sapiens, Staphylococcus aureus subsp. aureus
Chains: 12
Atoms: 16,684
Mol. weight: 238.96 kDa
Released: 14 Jun 2023

Explore 8D7K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8D7K contains 76 α-helices and 209 β-strands across 12 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: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	10
β-strand	33-34	2	9
α-helix	35-36	2
β-strand	43-48	6	11
β-strand	51-60	10	11
β-strand	63-66	4	11
α-helix	68-72	5
β-strand	80-83	4	11
β-strand	87	1	12
β-strand	96-105	10	11
β-strand	109	1	13
β-strand	114	1	13
β-strand	118-122	5	11
β-strand	136	1	9
α-helix	143-145	3
β-strand	149-154	6	9
β-strand	157	1	14
β-strand	164	1	14
β-strand	167	1	12
α-helix	168	1
β-strand	169-176	8	9
β-strand	185-188	4	9
β-strand	195	1	10
β-strand	204-207	4	9
β-strand	210-219	10	9
β-strand	229-233	5	9
α-helix	234-237	4
α-helix	238-245	8

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	158-165	8	3
β-strand	166	1	7
β-strand	169	1	7
β-strand	170-171	2	2
β-strand	174-179	6	3
β-strand	184-185	2	8
α-helix	187-202	16
α-helix	206-211	6
β-strand	216-221	6	3
β-strand	226-230	5	3
β-strand	235-237	3	9
β-strand	241-242	2	8
α-helix	243-245	3
β-strand	246-252	7	3

Chain C: 10 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	30-37	8	3
β-strand	40-50	11	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
α-helix	121-122	2
β-strand	123	1	6
α-helix	124-125	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	164-170	7
β-strand	179-182	4	2
β-strand	190	1	1
β-strand	199-201	3	2
β-strand	205	1	6
β-strand	206-213	8	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 D: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	25
β-strand	33-34	2	24
α-helix	35-36	2
β-strand	43-48	6	26
β-strand	51-60	10	26
β-strand	63-66	4	26
α-helix	68-71	4
α-helix	76-78	3
α-helix	79	1
β-strand	80-83	4	26
β-strand	87	1	27
β-strand	96-105	10	26
β-strand	109	1	28
β-strand	114	1	28
β-strand	118-122	5	26
β-strand	136	1	24
α-helix	143-145	3
β-strand	149-154	6	24
β-strand	157	1	29
β-strand	164	1	29
β-strand	167	1	27
β-strand	169-176	8	24
β-strand	185-188	4	24
β-strand	195	1	25
α-helix	203	1
β-strand	204-207	4	24
β-strand	210-219	10	24
α-helix	228	1
β-strand	229-233	5	24
α-helix	234-237	4
α-helix	238-244	7

Chain E: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	158-165	8	17
β-strand	166	1	22
β-strand	169	1	22
β-strand	170-171	2	16
β-strand	174-179	6	17
β-strand	184-185	2	23
α-helix	187-197	11
α-helix	198-202	5
α-helix	206-211	6
β-strand	216-221	6	17
β-strand	226-230	5	17
β-strand	235-237	3	24
β-strand	241-242	2	23
α-helix	243-245	3
β-strand	246-252	7	17

Chain F: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	15
β-strand	20-21	2	16
α-helix	22-23	2
β-strand	30-37	8	17
β-strand	40-50	11	17
β-strand	53-56	4	17
α-helix	58-60	3
β-strand	65-69	5	17
β-strand	73	1	18
β-strand	82-91	10	17
β-strand	96	1	19
β-strand	101	1	19
β-strand	105-109	5	17
β-strand	116	1	20
β-strand	119	1	20
β-strand	123	1	21
α-helix	124-125	2
β-strand	136-141	6	16
β-strand	153	1	18
β-strand	155-161	7	16
α-helix	162-163	2
α-helix	164-170	7
β-strand	179-182	4	16
β-strand	190	1	15
β-strand	199-201	3	16
β-strand	205	1	21
β-strand	206-213	8	16
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	16
α-helix	226-229	4
α-helix	230-237	8

Chain G: 6 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	36
β-strand	33-34	2	35
α-helix	35-36	2
β-strand	43-48	6	37
β-strand	51-60	10	37
β-strand	63-66	4	37
α-helix	68-70	3
α-helix	76-78	3
β-strand	80-83	4	37
β-strand	87	1	38
β-strand	96-105	10	37
β-strand	109	1	39
β-strand	114	1	39
β-strand	118-122	5	37
β-strand	149-154	6	35
β-strand	167	1	38
α-helix	168	1
β-strand	169-176	8	35
β-strand	185-188	4	35
β-strand	195	1	36
β-strand	204-207	4	35
β-strand	210-219	10	35
β-strand	229-233	5	35
α-helix	234-236	3
α-helix	238-244	7

Chain H: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	158-166	9	31
β-strand	169-171	3	31
β-strand	174-179	6	31
β-strand	184-185	2	34
α-helix	187-202	16
α-helix	206-211	6
β-strand	216-221	6	31
β-strand	226-230	5	31
β-strand	235-237	3	35
β-strand	241-242	2	34
α-helix	243-245	3
β-strand	246-252	7	31

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cathepsin G, C-terminal truncated form	C, F, I, L	protein	223	Homo sapiens	P08311 (AlphaFold model)
Extracellular Adherence Protein	B, E, H, K	protein	100	Staphylococcus aureus subsp. aureus	Q99QS1 (AlphaFold model)
Neutrophil elastase	A, D, G, J	protein	218	Homo sapiens	P08246 (AlphaFold model)

Sequence of entity 1 (C, F, I, L), FASTA

>8D7K_1 Cathepsin G, C-terminal truncated form (chains C, F, I, L)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR

Sequence of entity 2 (B, E, H, K), FASTA

>8D7K_2 Extracellular Adherence Protein (chains B, E, H, K)
GSTVQVPYTITVNGTSQNILSNLTFNKNQNISYKDLEGKVKSVLESNRGITDVDLRLSKQ
AKYTVNFKNGTKKVIDLKSGIYTANLINSSDIKSININVD

Sequence of entity 3 (A, D, G, J), FASTA

>8D7K_3 Neutrophil elastase (chains A, D, G, J)
IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNL
SRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGV
QCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCN
GLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ

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
9ASX 1.96 Å, BIFUNCTIONAL INHIBITION OF NEUTROPHIL ELASTASE AND CATHEPSIN G by Eap3 of S. aureus

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