1DVN: Latent form of plasminogen activator inhibitor-1

Latent form of plasminogen activator inhibitor-1 (pai-1). Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Sept 2000.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
1
Atoms
3,326
Mol. weight
42.82 kDa
Released
13 Sept 2000

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

Secondary structure: helices and β-sheets

1DVN contains 13 α-helices and 19 β-strands across 1 chain. 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, 19 β-strands

ElementResiduesLengthSheet
α-helix4-2623
β-strand3011
β-strand32-3432
α-helix36-4914
α-helix52-6211
α-helix71-8313
α-helix85-873
β-strand90-100113
α-helix105-1062
α-helix109-1179
β-strand122-12433
α-helix129-14315
β-strand163-174123
β-strand17514
α-helix178-1814
β-strand186-19055
β-strand196-20055
β-strand201-214142
β-strand220-22782
β-strand22814
β-strand233-24082
α-helix248-2514
α-helix256-2649
β-strand267-276102
β-strand278-28583
α-helix287-2926
α-helix297-2993
β-strand319-328103
β-strand332-343123
β-strand35411
β-strand357-36482
β-strand369-37792

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Plasminogen activator inhibitor-1Aprotein379Homo sapiensP05121 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1DVN_1 PLASMINOGEN ACTIVATOR INHIBITOR-1 (chains A)
VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQA
AMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRST
VKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFP
DSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP
YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR
QFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLF
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:

Browse structure collections

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