› › Structure analysis

The structure of an aldolase from Prochlorococcus marinus

X-ray diffraction
1.9Å resolution
PDB entry 3hjz coloured by chain, front view.
PDB entry 3hjz coloured by chain, side view.
PDB entry 3hjz coloured by chain, top view.
Source organism: Prochlorococcus marinus str. MIT 9312
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Quick links

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Assembly Name: Transaldolase
hide full assembly name
Multimeric state: monomeric
Accessible surface area: 15967.0 Å2
Buried surface area: 2645.38 Å2
Dissociation area: 97.54 Å2
Dissociation energy (ΔGdiss): -2.09 kcal/mol
Dissociation entropy (TΔSdiss): -0.38 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-174260
Monomeric assembly 1 of PDB entry 3hjz coloured by chemically distinct molecules, front view.
Monomeric assembly 1 of PDB entry 3hjz coloured by chemically distinct molecules, side view.
Monomeric assembly 1 of PDB entry 3hjz coloured by chemically distinct molecules, top view.
    Assembly 1
Confidence : 95%
No. subunits : 1
Symmetry : None
More details
3DComplex & QSbio predictionx
No. subunits : 1
Symmetry : None
Evidence : This biological assembly agrees with the prediction of both PISA & EPPIC

Macromolecules

Transaldolase
Chain: A
Length: 334 amino acids
Theoretical weight: 37.68 KDa
Source organism: Prochlorococcus marinus str. MIT 9312
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q31C15 (Residues: 1-333; Coverage: 100%)
Gene names: PMT9312_0519, tal
Pfam: Transaldolase/Fructose-6-phosphate aldolase
InterPro:
CATH: Aldolase class I
Transaldolase in PDB entry 3hjz, assembly 1, front view.
Transaldolase in PDB entry 3hjz, assembly 1, side view.
Transaldolase in PDB entry 3hjz, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q31C15  
133450100150200250300
 
100200300G*KSILEQLSS*TVVVADTGDLDSIKKFQPRDATTNPSLILAAAKNPDYVKLIDKAIESSENTLPNGFSEIELIKETVDQVSVFFGKEILKIISGRVSTEVDARLSFDTEATVKKARKLINLYKNFGIEKERILIKIAATWEGIKAAEILEKEGIKCNLTLLFNFCQAVTCANANITLISPFVGRILDWHKAKTGKTSFIGAEDPGVISVTQIYKYFKEKGFKTEV*GASFRNLDEIKELAGCDLLTIAPKFLEELKREKGVLIRKLDASTKINNSIDYKFEEKDFRLS*LEDQ*ASEKLSEGITGFSKAIEELEELLIERLSE*KNHKLISAN
UniProt
Q31C15
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation
Molecule details ›

Search similar proteins

Quick links