8D4S: Cathepsin G Inhibited by Eap1 from S. aureus

Crystal Structure of Cathepsin G Inhibited by Eap1 from S. aureus. Determined by X-ray diffraction at 1.95 Å resolution. Released 21 Dec 2022.

Method: X-ray diffraction
Resolution: 1.95 Å
Organisms: Homo sapiens, Staphylococcus aureus subsp. aureus Mu50
Chains: 8
Atoms: 10,684
Mol. weight: 147.22 kDa
Ligands: NAG
Released: 21 Dec 2022

Explore 8D4S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8D4S contains 46 α-helices and 124 β-strands across 8 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, 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	65-69	5	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
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
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

Chains B, D and H: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	48-57	10	3
β-strand	60	1	3
β-strand	61-62	2	2
β-strand	65-71	7	3
β-strand	75-77	3	26
α-helix	78-93	16
α-helix	97-102	6
β-strand	106-112	7	3
β-strand	117-121	5	3
β-strand	131-133	3	26
α-helix	134-136	3
β-strand	137-144	8	3

Chain C: 9 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	30-36	7	9
β-strand	42-50	9	9
β-strand	53-56	4	9
α-helix	58-60	3
β-strand	64-69	6	9
β-strand	73	1	10
β-strand	82-91	10	9
β-strand	96	1	11
β-strand	101	1	11
β-strand	105-109	5	9
β-strand	116	1	12
β-strand	119	1	12
β-strand	123	1	8
α-helix	125-126	2
β-strand	136-141	6	8
β-strand	153	1	10
β-strand	155-161	7	8
α-helix	162-163	2
α-helix	164-170	7
β-strand	179-182	4	8
β-strand	190	1	7
β-strand	199-202	4	8
β-strand	205-213	9	8
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	8
α-helix	226-229	4
α-helix	230-237	8

Chain E: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	13
β-strand	20-21	2	14
α-helix	22-23	2
β-strand	30-37	8	15
β-strand	40-50	11	15
β-strand	53-56	4	15
α-helix	58-60	3
β-strand	64-69	6	15
β-strand	73	1	16
β-strand	82-91	10	15
β-strand	96	1	17
β-strand	101	1	17
β-strand	105-109	5	15
β-strand	116	1	18
β-strand	119	1	18
β-strand	123	1	14
α-helix	125-126	2
β-strand	136-141	6	14
β-strand	153	1	16
β-strand	155-161	7	14
α-helix	162-163	2
α-helix	164-170	7
β-strand	179-182	4	14
β-strand	190	1	13
β-strand	199-202	4	14
β-strand	205-213	9	14
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	14
α-helix	226-229	4
α-helix	230-236	7

Chain F: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	48-57	10	15
β-strand	60	1	15
β-strand	61-62	2	14
β-strand	65-71	7	15
β-strand	75-76	2	25
α-helix	78-93	16
α-helix	97-102	6
β-strand	106-112	7	15
β-strand	117-121	5	15
β-strand	132-133	2	25
α-helix	134-136	3
β-strand	137-144	8	15

Chain G: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	19
β-strand	20-21	2	20
α-helix	22-23	2
β-strand	30-37	8	21
β-strand	40-50	11	21
β-strand	53-56	4	21
α-helix	58-60	3
β-strand	65-69	5	21
β-strand	73	1	22
β-strand	82-91	10	21
β-strand	96	1	23
β-strand	101	1	23
β-strand	105-109	5	21
β-strand	116	1	24
β-strand	119	1	24
β-strand	123	1	20
α-helix	124-126	3
β-strand	136-141	6	20
β-strand	153	1	22
β-strand	155-161	7	20
α-helix	164-170	7
β-strand	179-182	4	20
β-strand	190	1	19
β-strand	199-202	4	20
β-strand	205-213	9	20
α-helix	218	1
α-helix	220	1
β-strand	221-225	5	20
α-helix	226-229	4
α-helix	230-237	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cathepsin G, C-terminal truncated form	A, C, E, G	protein	223	Homo sapiens	P08311 (AlphaFold model)
Extracellular Adherence Protein	B, D, F, H	protein	100	Staphylococcus aureus subsp. aureus Mu50	Q99QS1 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>8D4S_1 Cathepsin G, C-terminal truncated form (chains A, C, E, G)
IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ
RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT
LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD
SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR

Sequence of entity 2 (B, D, F, H), FASTA

>8D4S_2 Extracellular Adherence Protein (chains B, D, F, H)
GSTIQIPYTITVNGTSQNILSSLTFNKNQNISYKDIENKVKSVLYFNRGISDIDLRLSKQ
AEYTVHFKNGTKRVIDLKSGIYTADLINTSDIKAISVNVD

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Characterization of two distinct neutrophil serine protease-binding modes within a Staphylococcus aureus innate immune evasion protein family. Gido, C.D., Herdendorf, T.J., Geisbrecht, B.V. J Biol Chem (2023) 299:102969-102969. DOI 10.1016/j.jbc.2023.102969 · 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…
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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