1BBR: Epsilon-thrombin

The structure of residues 7-16 of the a alpha chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution. Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Jan 1994.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Bos taurus, Homo sapiens
Chains: 10
Atoms: 8,084
Mol. weight: 109.68 kDa
Released: 31 Jan 1994

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

Secondary structure: helices and β-sheets

1BBR contains 36 α-helices and 76 β-strands across 10 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 E: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	149D	1	7
β-strand	151	1	7
β-strand	154	1	5
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-171	7
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	231-242	12

Chains F and G: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	316-317	2	2

Chain H: 8 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-35	6	3
β-strand	39-46	8	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	81-90	10	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

Chain I: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	310-313	4
β-strand	316-317	2	17

Chain J: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	14C-14K	9

Chain K: 9 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	8
β-strand	20-21	2	9
α-helix	22-23	2
β-strand	30-35	6	10
β-strand	40-46	7	10
β-strand	51-54	4	10
α-helix	56-58	3
β-strand	60-60A	2	11
α-helix	60B-60D	3
β-strand	60F-60G	2	11
β-strand	64-68	5	10
β-strand	72	1	12
β-strand	81-83	3	10
β-strand	85-90	6	10
β-strand	95	1	13
β-strand	100	1	13
β-strand	104-108	5	10
α-helix	111-114	4
β-strand	115	1	14
β-strand	118	1	14
α-helix	120-121	2
β-strand	122	1	9
α-helix	123-125	3
α-helix	126-129C	7
β-strand	135-140	6	9
β-strand	149A	1	15
β-strand	149D	1	15
β-strand	154	1	12
β-strand	156-162	7	9
α-helix	165-171	7
β-strand	180-183	4	9
β-strand	189	1	8
β-strand	198-202	5	9
β-strand	207-216	10	9
β-strand	226-230	5	9
α-helix	231-242	12

Chain L: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	14C-14I	7

Chain M: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	1F-1C	4
α-helix	8-10	3
α-helix	14C-14H	6

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
Epsilon-thrombin	J, L, M	protein	49	Bos taurus	P00735 (AlphaFold model)
Epsilon-thrombin	H	protein	150	Bos taurus	P00735 (AlphaFold model)
Epsilon-thrombin	E	protein	109	Bos taurus	P00735 (AlphaFold model)
Fibrinogen alpha/alpha-E chain precursor	F, G, I	protein	11	Homo sapiens	P02671 (AlphaFold model)
Epsilon-thrombin	K, N	protein	259	Bos taurus	P00735 (AlphaFold model)

Sequence of entity 1 (J, L, M), FASTA

>1BBR_1 EPSILON-THROMBIN (chains J, L, M)
TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR

Sequence of entity 2 (H), FASTA

>1BBR_2 EPSILON-THROMBIN (chains H)
IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL
VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL
PDKQTAAKLLHAGFKGRVTGWGNRRETWTT

Sequence of entity 3 (E), FASTA

>1BBR_3 EPSILON-THROMBIN (chains E)
SVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFV
MKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS

Sequence of entity 4 (F, G, I), FASTA

>1BBR_4 FIBRINOGEN ALPHA/ALPHA-E CHAIN PRECURSOR (chains F, G, I)
XDFLAEGGGVR

Sequence of entity 5 (K, N), FASTA

>1BBR_5 EPSILON-THROMBIN (chains K, N)
IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL
VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL
PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR
ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDRLGS

Primary citation

The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution. Martin, P.D., Robertson, W., Turk, D. et al. J Biol Chem (1992) 267:7911-7920. PubMed

Other PDB entries of the same protein (UniProt P00735 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7A0D 1.6 Å, The Crystal Structure of Bovine Thrombin in complex with Hirudin (C16U/C28U) at 1.6…
1NL1 1.9 Å, Bovine prothrombin fragment 1 in complex with calcium ion
7A0E 1.9 Å, The Crystal Structure of Bovine Thrombin in complex with Hirudin (C6U/C14U) at 1.9…
1ETR 2.2 Å, Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the…
1MKX 2.2 Å, The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement…
1UCY 2.2 Å, Thrombin complexed with fibrinopeptide a alpha (residues 7-19). Three complexes, one…
2PF2 2.2 Å, The CA+2 ion and membrane binding structure of the gla domain of ca-prothrombin fragment 1
3PMA 2.2 Å, 2.2 Angstrom crystal structure of the complex between Bovine Thrombin and Sucrose…
1ETS 2.3 Å, Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the…
1MKW 2.3 Å, The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement…
1NL2 2.3 Å, Bovine prothrombin fragment 1 in complex with calcium and lysophosphotidylserine
2ODY 2.35 Å, Thrombin-bound boophilin displays a functional and accessible reactive-site loop

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