4DCB: Y. pestis Plasminogen Activator Pla

Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11. Determined by X-ray diffraction at 2.03 Å resolution. Released 6 Jun 2012.

Method
X-ray diffraction
Resolution
2.03 Å
Organisms
Yersinia pestis, Homo sapiens
Chains
2
Atoms
2,447
Mol. weight
35.5 kDa
Ligands
PO4, C8E, MRD
Released
6 Jun 2012

Explore 4DCB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4DCB contains 3 α-helices and 14 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: 3 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix6-83
α-helix11-133
β-strand14-32191
β-strand39-62241
β-strand65-74101
β-strand78-8691
β-strand97-122261
β-strand126-144191
β-strand147-15041
β-strand155-15841
α-helix159-1602
β-strand164-185221
β-strand188-208211
β-strand213-234221
β-strand239-250121
β-strand255-25951
β-strand275-291171

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Coagulase/fibrinolysinAprotein297Yersinia pestisP17811 (AlphaFold model)
PlasminogenFprotein11Homo sapiensP00747 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4DCB_1 Coagulase/fibrinolysin (chains A)
LIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNVAILKGDISWDPYSF
LTLNARGWTSLASGSGNMDNYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWLLQDE
NYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYR
INDFELNALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAE
FTYSKYDEGKGGTQTIDKNSGDSVSIGGDAAGISNKNYTVTAGLQYRFGGGHHHHHH
Sequence of entity 2 (F), FASTA
>4DCB_2 Plasminogen (chains F)
KCPGRVVGGCK

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1
C8E(hydroxyethyloxy)tri(ethyloxy)octaneC16 H34 O51
MRD(4R)-2-methylpentane-2,4-diolC6 H14 O24

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

Primary citation

Structural basis for activation of an integral membrane protease by lipopolysaccharide. Eren, E., van den Berg, B. J Biol Chem (2012) 287:23971-23976. DOI 10.1074/jbc.M112.376418 · PubMed

Other PDB entries of the same protein (UniProt P17811 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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