1DVM: Active form of human pai-1

Active form of human pai-1. Determined by X-ray diffraction at 2.4 Å resolution. Released 6 Sept 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,383
Mol. weight: 171.32 kDa
Released: 6 Sept 2000

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

Secondary structure: helices and β-sheets

1DVM contains 55 α-helices and 71 β-strands across 4 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: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	5-27	23
β-strand	32-34	3	1
α-helix	38-46	9
α-helix	47-49	3
α-helix	52-62	11
α-helix	71-82	12
β-strand	91-100	10	2
α-helix	109-117	9
β-strand	122-124	3	2
α-helix	129-142	14
α-helix	153-156	4
β-strand	163-172	10	2
β-strand	175	1	3
β-strand	185-190	6	1
β-strand	196-214	19	1
β-strand	220-227	8	1
β-strand	228	1	3
α-helix	229-231	3
β-strand	233-240	8	1
α-helix	248-251	4
α-helix	256-265	10
β-strand	267-276	10	1
β-strand	278-284	7	2
α-helix	287-291	5
α-helix	297-299	3
β-strand	319-328	10	2
β-strand	350-353	4	1
β-strand	358-364	7	1
β-strand	369-376	8	1

Chain B: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	5-24	20
β-strand	32-34	3	4
α-helix	36-46	11
α-helix	52-62	11
α-helix	71-82	12
β-strand	91-100	10	5
α-helix	104-106	3
α-helix	109-117	9
β-strand	122-124	3	5
α-helix	129-142	14
α-helix	152-156	5
β-strand	163-172	10	5
β-strand	175	1	6
α-helix	178-180	3
β-strand	185-190	6	4
β-strand	196-214	19	4
β-strand	220-227	8	4
β-strand	228	1	6
α-helix	229-231	3
β-strand	233-240	8	4
α-helix	248-251	4
α-helix	256-264	9
β-strand	267-276	10	4
β-strand	278-285	8	5
α-helix	287-292	6
α-helix	297-299	3
β-strand	319-328	10	5
β-strand	352-353	2	4
β-strand	358-364	7	4
β-strand	369-376	8	4

Chain C: 12 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-24	19
β-strand	32-34	3	7
α-helix	36-46	11
α-helix	52-62	11
α-helix	71-82	12
β-strand	91-100	10	8
β-strand	105	1	9
α-helix	106	1
α-helix	109-117	9
β-strand	122-124	3	8
α-helix	129-143	15
α-helix	152-155	4
β-strand	163-172	10	8
β-strand	175	1	10
β-strand	185	1	7
β-strand	188-190	3	11
β-strand	196-198	3	11
β-strand	201-214	14	7
β-strand	220-227	8	7
β-strand	228	1	10
β-strand	233-240	8	7
α-helix	248-251	4
α-helix	256-264	9
β-strand	267-276	10	7
β-strand	278-285	8	8
α-helix	287-291	5
α-helix	297-299	3
β-strand	310	1	9
β-strand	319-328	10	8
β-strand	351-353	3	7
β-strand	358-364	7	7
β-strand	370-376	7	7

Chain D: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	8-24	17
β-strand	32-34	3	12
α-helix	36-49	14
α-helix	52-62	11
α-helix	71-82	12
β-strand	91-100	10	13
α-helix	104-106	3
α-helix	109-117	9
β-strand	122-124	3	13
α-helix	129-143	15
α-helix	152-155	4
β-strand	163-171	9	13
β-strand	175	1	14
α-helix	181-183	3
β-strand	185-186	2	12
α-helix	188	1
β-strand	189-190	2	15
α-helix	191	1
β-strand	196-197	2	15
β-strand	200-214	15	12
β-strand	220-227	8	12
β-strand	228	1	14
α-helix	229-231	3
β-strand	233-239	7	12
α-helix	248-251	4
α-helix	256-263	8
β-strand	268-276	9	12
β-strand	278-285	8	13
α-helix	287-291	5
α-helix	297-299	3
β-strand	319-328	10	13
β-strand	342-346	5	2
β-strand	350-353	4	12
β-strand	358-364	7	12
β-strand	369-376	8	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Plasminogen activator inhibitor-1	A, B, C, D	protein	379	Homo sapiens	P05121 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1DVM_1 PLASMINOGEN ACTIVATOR INHIBITOR-1 (chains A, B, C, D)
VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQA
AMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRST
VKQVDFSEVERARFIINDWVKTHTKGMISHLLGTGAVQQLTRLVLVNALYFNGQWKTPFP
DSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP
YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR
QFQADFTSLSDQEPLHVALALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIIDRPFLF
VVRHNPTGTVLFMGQVMEP

Primary citation

Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Stout, T.J., Graham, H., Buckley, D.I. et al. Biochemistry (2000) 39:8460-8469. DOI 10.1021/bi000290w · PubMed

Other PDB entries of the same protein (UniProt P05121 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7AQF 1.77 Å, Crystal Structure of Small Molecule Inhibitor TM5484 Bound to Stabilized Active…
1LJ5 1.8 Å, 1.8A Resolution Structure of Latent Plasminogen Activator Inhibitor-1(PAI-1)
6ZRV 1.88 Å, Crystal Structure of Stabilized Active Plasminogen Activator Inhibitor-1 (PAI-1-W175F)…
1A7C 1.95 Å, Human plasminogen activator inhibitor type-1 in complex with a pentapeptide
3CVM 2.02 Å, High resolution structure of a stable Plasminogen activator inhibitor type-1 in its…
6GWN 2.03 Å, Crystal Structure of Stabilized Active Plasminogen Activator Inhibitor-1 (PAI-1-W175F)…
1DVN 2.1 Å, Latent form of plasminogen activator inhibitor-1 (pai-1)
4G8R 2.19 Å, Crystal Structure of a novel small molecule inactivator bound to plasminogen activator…
7AQG 2.27 Å, Crystal Structure of Small Molecule Inhibitor TM5484 Bound to Stabilized Active…
1OC0 2.28 Å, plasminogen activator inhibitor-1 complex with somatomedin B domain of vitronectin
6GWP 2.28 Å, Crystal Structure of Stabilized Active Plasminogen Activator Inhibitor-1 (PAI-1-stab) in…
3PB1 2.3 Å, Crystal Structure of a Michaelis Complex between Plasminogen Activator Inhibitor-1 and…

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