8G25: Cathepsin-G

Crystal Structure of Cathepsin-G and Neutrophil Elastase Inhibited by S. aureus EapH2 at pH 7.5. Determined by X-ray diffraction at 1.8 Å resolution. Released 26 Apr 2023.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Homo sapiens, Staphylococcus aureus subsp. aureus Mu50
Chains: 9
Atoms: 13,335
Mol. weight: 185.52 kDa
Released: 26 Apr 2023

Explore 8G25 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G25 contains 51 α-helices and 156 β-strands across 9 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, 22 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
β-strand	116	1	6
β-strand	119	1	6
β-strand	123	1	2
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	165-168	4
β-strand	179-182	4	2
β-strand	190	1	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: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	7
β-strand	33-34	2	8
α-helix	35-36	2
β-strand	43-48	6	9
β-strand	51-60	10	9
β-strand	63-66	4	9
α-helix	68-71	4
α-helix	76-78	3
β-strand	80-83	4	9
β-strand	87	1	10
β-strand	96-105	10	9
β-strand	109	1	11
β-strand	114	1	11
β-strand	118-122	5	9
α-helix	126-128	3
β-strand	149-154	6	8
β-strand	157	1	12
β-strand	164	1	12
β-strand	167	1	10
β-strand	169-176	8	8
β-strand	185-188	4	8
β-strand	195	1	7
β-strand	204-207	4	8
β-strand	210-219	10	8
β-strand	229-233	5	8
α-helix	234-237	4
α-helix	238-245	8

Chain C: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	45-54	10	3
β-strand	57	1	3
β-strand	58-59	2	2
β-strand	62-68	7	3
β-strand	72-73	2	13
α-helix	75-90	16
α-helix	94-98	5
β-strand	102-109	8	3
β-strand	114-118	5	3
β-strand	123-125	3	8
β-strand	129-130	2	13
α-helix	131-133	3
β-strand	134-142	9	3

Chain D: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	46-54	9	14
β-strand	57	1	14
β-strand	58-59	2	15
β-strand	62-67	6	14
β-strand	72-73	2	16
α-helix	75-90	16
α-helix	94-98	5
β-strand	102-109	8	14
β-strand	114-118	5	14
β-strand	123-125	3	17
β-strand	129-130	2	16
α-helix	131-133	3
β-strand	134-142	9	14

Chain E: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	18
α-helix	35-36	2
β-strand	43-48	6	19
β-strand	52-60	9	19
β-strand	63-66	4	19
α-helix	69-71	3
β-strand	79-83	5	19
β-strand	87	1	20
β-strand	96-98	3	19
β-strand	100-105	6	19
β-strand	109	1	21
β-strand	114	1	21
β-strand	118-122	5	19
α-helix	126-128	3
β-strand	149-154	6	17
β-strand	157	1	22
β-strand	164	1	22
β-strand	167	1	20
α-helix	168	1
β-strand	169-176	8	17
β-strand	185-188	4	17
β-strand	195	1	18
β-strand	204-207	4	17
β-strand	210-219	10	17
β-strand	229-233	5	17
α-helix	234-237	4
α-helix	238-245	8

Chain F: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	23
α-helix	20	1
β-strand	21	1	15
α-helix	22-23	2
β-strand	30-37	8	14
β-strand	40-50	11	14
β-strand	53-56	4	14
α-helix	58-60	3
β-strand	64-69	6	14
β-strand	73	1	24
β-strand	82-91	10	14
β-strand	96	1	25
β-strand	101	1	25
β-strand	105-109	5	14
β-strand	116	1	26
β-strand	119	1	26
β-strand	136-141	6	15
β-strand	153	1	24
β-strand	155-161	7	15
α-helix	162-163	2
α-helix	165-168	4
β-strand	179-182	4	15
β-strand	190	1	23
β-strand	199-201	3	15
β-strand	206-213	8	15
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	15
α-helix	226-229	4
α-helix	230-237	8

Chain G: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	44-54	11	27
β-strand	57	1	27
β-strand	58-59	2	28
β-strand	62-68	7	27
β-strand	72-73	2	29
α-helix	75-90	16
α-helix	94-98	5
β-strand	102-109	8	27
β-strand	114-118	5	27
β-strand	123-125	3	30
β-strand	129-130	2	29
α-helix	131-133	3
β-strand	134-142	9	27

Chain H: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	30	1	31
β-strand	33-34	2	30
α-helix	35-36	2
β-strand	43-48	6	32
β-strand	51-60	10	32
β-strand	63-66	4	32
α-helix	68-71	4
β-strand	80-83	4	32
β-strand	87	1	33
β-strand	96-97	2	32
β-strand	100-105	6	32
β-strand	109	1	34
β-strand	114	1	34
β-strand	118-122	5	32
β-strand	149-154	6	30
β-strand	157	1	35
β-strand	164	1	35
β-strand	167	1	33
β-strand	169-176	8	30
β-strand	185-188	4	30
β-strand	195	1	31
β-strand	204-207	4	30
β-strand	210-219	10	30
β-strand	229-232	4	30
α-helix	234-237	4
α-helix	238-244	7

1 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	A, F, I	protein	223	Homo sapiens	P08311 (AlphaFold model)
Neutrophil elastase	B, E, H	protein	218	Homo sapiens	P08246 (AlphaFold model)
MAP domain-containing protein	C, D, G	protein	117	Staphylococcus aureus subsp. aureus Mu50	A0A0H3JUK5 (AlphaFold model)

Sequence of entity 1 (A, F, I), FASTA

>8G25_1 Cathepsin-G (chains A, F, I)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR

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

>8G25_2 Neutrophil elastase (chains B, E, H)
IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNL
SRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGV
QCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCN
GLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQ

Sequence of entity 3 (C, D, G), FASTA

>8G25_3 MAP domain-containing protein (chains C, D, G)
GSTAEKDKLPATQKAKEMQNVPYTIAVDGIMAFNQSYLNLPKDSQLSYLDLGNKVKALLY
DERGVTPEKIRNAKSAVYTITWKDGSKKEVDLKKDSYTANLFDSNSIKQIDINVKTK

Primary citation

Simultaneous inhibition of two neutrophil serine proteases by the S. aureus innate immune evasion protein EapH2. Mishra, N., Herdendorf, T.J., Prakash, O. et al. J Biol Chem (2023) 299:104878-104878. DOI 10.1016/j.jbc.2023.104878 · 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
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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