1GJ4: Thrombin

Selectivity at S1, H2O displacement, upa, tpa, SER190/ALA190 protease, structure-based drug design. Determined by X-ray diffraction at 1.81 Å resolution. Released 27 Apr 2002.

Method: X-ray diffraction
Resolution: 1.81 Å
Organisms: Homo sapiens, Hirudo medicinalis
Chains: 3
Atoms: 2,681
Mol. weight: 35.62 kDa
Ligands: 132
Released: 27 Apr 2002

Explore 1GJ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GJ4 contains 15 α-helices and 23 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 H: 11 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
β-strand	30-35	6	3
β-strand	40-46	7	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	60-60A	2	4
α-helix	60B-60D	3
β-strand	60F-60G	2	4
α-helix	61-63	3
β-strand	64-68	5	3
β-strand	72	1	5
β-strand	81-83	3	3
β-strand	85-90	6	3
β-strand	95	1	6
β-strand	100	1	6
β-strand	104-108	5	3
α-helix	111-114	4
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-124	2
α-helix	126-129C	7
β-strand	135-140	6	2
β-strand	154	1	5
β-strand	156-162	7	2
α-helix	165-169	5
α-helix	175-176	2
β-strand	180-183	4	2
α-helix	186-186B	3
β-strand	189	1	1
β-strand	198-202	5	2
β-strand	207-216	10	2
β-strand	226-230	5	2
α-helix	231-245	15

Chain I: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	56-58	3
α-helix	61-63	3

Chain L: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	14C-14I	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Thrombin	L	protein	36	Homo sapiens	P00734 (AlphaFold model)
Thrombin	H	protein	258	Homo sapiens	P00734 (AlphaFold model)
Acetyl hirudin	I	protein	11	Hirudo medicinalis	P28504 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1GJ4_1 THROMBIN (chains L)
TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR

Sequence of entity 2 (H), FASTA

>1GJ4_2 THROMBIN (chains H)
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLL
VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL
PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR
ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFG

Sequence of entity 3 (I), FASTA

>1GJ4_3 ACETYL HIRUDIN (chains I)
DFEEIPEEYLQ

Ligands and cofactors

ID	Name	Formula	Copies
132	6-chloro-2-(2-hydroxy-biphenyl-3-yl)-1H-indole-5-carboxamidine	C21 H17 Cl N3 O	1

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

Primary citation

Engineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets. Katz, B.A., Sprengeler, P.A., Luong, C. et al. Chem Biol (2001) 8:1107-1121. DOI 10.1016/S1074-5521(01)00084-9 · PubMed

Other PDB entries of the same protein (UniProt P00734 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5AFY 1.12 Å, Thrombin in complex with 3-chloro-benzamide
4UD9 1.12 Å, Thrombin in complex with 5-chlorothiophene-2-carboxamide
4UE7 1.13 Å, Thrombin in complex with 1-amidinopiperidine
4UDW 1.16 Å, Thrombin in complex with 1-(2R)-2-amino-3-phenyl-propanoyl-N-(2,…
4UEH 1.16 Å, Thrombin in complex with benzamidine
5AF9 1.18 Å, Thrombin in complex with 4-Methoxy-N-(2-pyridinyl)benzamide
3RM2 1.23 Å, Human Thrombin in complex with MI003
5AHG 1.24 Å, Thrombin in complex with ((4-chlorophenyl)sulfamoyl))diemethylamine
2BVR 1.25 Å, Human thrombin complexed with fragment-based small molecules occupying the S1 pocket
3VXE 1.25 Å, Human alpha-thrombin-Bivalirudin complex at PD5.0
2UUF 1.26 Å, Thrombin-hirugen binary complex at 1.26A resolution
3SI4 1.27 Å, Human Thrombin In Complex With UBTHR104

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