wwPDB validation report of PDB entry 2X1T

A MONOMERIC MUTANT OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, WHICH HAS AN EMPTY ACTIVE SITE IN BOTH ASYMMETRIC UNITS

THE A178L MUTATION IN THE C-TERMINAL HINGE OF THE FLEXIBLE LOOP-6 OF TRIOSEPHOSPHATE ISOMERASE (TIM) INDUCES A MORE CLOSED CONFORMATION OF THIS HINGE REGION IN DIMERIC AND MONOMERIC TIM

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TIM WITH THE SALT-BRIDGE-FORMING RESIDUE ARG191 MUTATED TO SER

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3- PHOSPHOGLYCERATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH GLYCEROL -3-PHOSPHATE

CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE

STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATEISOMERASE COMPLEXED WITH 3- PHOSPHONOPROPIONATE

CRYSTAL STRUCTURE OF TRIOSE-PHOSPHATE ISOMERASE WITH MODIFIED SUBSTRATE BINDING SITE

MOL_ID: 1; MOLECULE: TRIOSEPHOSPHATE ISOMERASE ; CHAIN: NULL; EC: 5.3.1.1; MUTATION: VARIANT OF MONOTIM WITH PHE 45 REPLACED BY SER AND VAL 46 REPLACED BY SER (F45S, V46S) AND 73 - 79 DELETED

STRUCTURE-BASED ENZYME ENGINEERING EFFORTS WITH AN INACTIVE MONOMERIC TIM VARIANT: THE IMPORTANCE OF A SINGLE POINT MUTATION FOR GENERATING AN ACTIVE SITE WITH SUITABLE BINDING PROPERTIES

STRUCTURES OF THE OPEN AND CLOSED STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH 2- PHOSPHOGLYCERATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH SULFATE

TRIOSEPHOSPHATE ISOMERASE COMPLEX WITH N- HYDROXY-4-PHOSPHONO-BUTANAMIDE

TRIOSEPHOSPHATE ISOMERASE MUTANT WITH PHE 45 REPLACED BY SER, VAL 46 REPLACED BY SER, AND RESIDUES 68 - 82 REPLACED BY THE RESIDUES GNADALAS (F45S,V46S,68-82:GNADALAS)

THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE

PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATEISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OFA SEVEN RESIDUE LOOP

TRIOSEPHOSPHATE ISOMERASE MUTANT WITH 15 RESIDUES (68 - 82) REPLACED BY 8 RESIDUES

MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE

MOL_ID: 1; MOLECULE: TRIOSEPHOSPHATE ISOMERASE ; CHAIN: NULL; EC: 5.3.1.1; ENGINEERED: YES; MUTATION: I68G, A69N, K70A, S71D, DEL( 73-79), P81A, A100W; OTHER_DETAILS: MONOTIM WITH A110W MUTATION

ENGINEERED RESIDUE IN CHAIN A, ASN 15 TO SER ENGINEERED RESIDUE IN CHAIN A, GLN 18 TO PRO ENGINEERED RESIDUE IN CHAIN A, GLN 19 TO ASP ENGINEERED RESIDUE IN CHAIN A, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN A, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN A, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN A, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN A, GLY 72 TO ALA ENGINEERED RESIDUE IN CHAIN A, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN A, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN A, ALA 100 TO TRP ENGINEERED RESIDUE IN CHAIN A, VAL 233 TO ALA ENGINEERED RESIDUE IN CHAIN B, ASN 15 TO SER ENGINEERED RESIDUE IN CHAIN B, GLN 18 TO PRO ENGINEERED RESIDUE IN CHAIN B, GLN 19 TO ASP ENGINEERED RESIDUE IN CHAIN B, ILE 68 TO GLY ENGINEERED RESIDUE IN CHAIN B, ALA 69 TO ASN ENGINEERED RESIDUE IN CHAIN B, LYS 70 TO ALA ENGINEERED RESIDUE IN CHAIN B, SER 71 TO ASP ENGINEERED RESIDUE IN CHAIN B, GLY 72 TO ALA ENGINEERED RESIDUE IN CHAIN B, PRO 81 TO ALA ENGINEERED RESIDUE IN CHAIN B, ILE 82 TO SER ENGINEERED RESIDUE IN CHAIN B, ALA 100 TO TRP ENGINEERED RESIDUE IN CHAIN B, VAL 233 TO ALA

RESIDUES 14-19 IN MOLECULE A ARE DISORDERED.

TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL (E.C.5.3.1.1)

The largest off-origin peak in the Patterson function is 5.47% of the height of the origin peak. No significant pseudotranslation is detected.

20191225.v01 (using entries in the PDB archive December 25th 2019)

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures