1BDA: Single chain tissue type plasminogen activator

Catalytic domain of human single chain tissue plasminogen activator in complex with dansyl-egr-cmk (dansyl-glu-gly-arg chloromethyl ketone). Determined by X-ray diffraction at 3.35 Å resolution. Released 11 May 1999.

Method: X-ray diffraction
Resolution: 3.35 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,271
Mol. weight: 60.71 kDa
Ligands: 2Z0
Released: 11 May 1999

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

Secondary structure: helices and β-sheets

1BDA contains 20 α-helices and 46 β-strands across 2 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: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	1	1	1
β-strand	15-16	2	2
β-strand	19-21	3	2
α-helix	24-26	3
β-strand	30-36	7	3
β-strand	38-48	11	3
β-strand	51-54	4	3
α-helix	57-59	3
α-helix	61-63	3
β-strand	64-68	5	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	95	1	5
β-strand	100	1	5
β-strand	104-109	6	3
α-helix	113-114	2
β-strand	120	1	1
α-helix	121	1
β-strand	122	1	2
α-helix	123-125	3
β-strand	135-140	6	2
β-strand	143	1	6
β-strand	151	1	6
β-strand	154	1	4
β-strand	156-162	7	2
α-helix	163-164	2
α-helix	165-167	3
β-strand	180-184	5	2
β-strand	198-203	6	2
β-strand	206-215	10	2
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-240	6

Chain B: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	15-16	2	7
β-strand	19-21	3	7
α-helix	24-26	3
β-strand	30-35	6	8
β-strand	40-48	9	8
β-strand	51-55	5	8
α-helix	57-59	3
α-helix	61-63	3
β-strand	64-68	5	8
β-strand	72	1	9
β-strand	81-90	10	8
β-strand	95	1	10
β-strand	100	1	10
β-strand	103-109	7	8
α-helix	113-114	2
β-strand	115	1	11
β-strand	118	1	11
α-helix	120-121	2
β-strand	122	1	7
α-helix	123-125	3
α-helix	130-131	2
β-strand	135-140	6	7
β-strand	143	1	12
β-strand	151	1	12
β-strand	154	1	9
β-strand	156-162	7	7
α-helix	163-164	2
α-helix	165-167	3
β-strand	180-184	5	7
β-strand	198-203	6	7
β-strand	206-215	10	7
β-strand	226-230	5	7
α-helix	231-240	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Single chain tissue type plasminogen activator	A, B	protein	265	Homo sapiens	P00750 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1BDA_1 SINGLE CHAIN TISSUE TYPE PLASMINOGEN ACTIVATOR (chains A, B)
TCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAH
CFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSS
RCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCT
SQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGC
GQKDVPGVYTKVTNYLDWIRDNMRP

Ligands and cofactors

ID	Name	Formula	Copies
2Z0	N-{[5-(dimethylamino)naphthalen-2-yl]sulfonyl}-L-alpha-glutamyl-N-[(1S)-4-{[ami…	C26 H37 Cl N7 O7 S	2

Primary citation

Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA. Renatus, M., Engh, R.A., Stubbs, M.T. et al. EMBO J (1997) 16:4797-4805. DOI 10.1093/emboj/16.16.4797 · PubMed

Other PDB entries of the same protein (UniProt P00750 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RTF 2.3 Å, Complex of benzamidine with the catalytic domain of human two chain tissue plasminogen…
1PML 2.38 Å, Kringle-kringle interactions in multimer kringle structures
1TPK 2.4 Å, Crystal structure of the kringle-2 domain of tissue plasminogen activator at 2.4-Å…
1A5H 2.9 Å, Catalytic domain of human two-chain tissue plasminogen activator complex of a…
5BRR 3.16 Å, Michaelis complex of tPA-S195A:PAI-1
5ZLZ 3.58 Å, Structure of tPA and PAI-1
1PK2 Solution structure of the tissue-type plasminogen activator kringle 2 domain complexed…
1TPG F1-G module pair residues 1-91 (C83S) of tissue-type plasminogen activator (T-pa) (NMR,…
1TPM Solution structure of the fibrin binding finger domain of tissue-type plasminogen…
1TPN Solution structure of the fibrin binding finger domain of tissue-type plasminogen…

Browse structure collections

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