Probing the active center of catalase-phenol oxidase from Scytalidium thermophilum

CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE

PROTEIN CRYSTAL WAS OBTAINED IN 6-16 % PEG400, 0.2 M POTASSIUM CHLORIDE, 0.01 M CALCIUM CHLORIDE DEHYDRATE AND 0.05 M SODIUM CACODYLATE TRIHYDRATE AT PH 5.2

CRYSTAL STRUCTURE, RECOMBINANT EXPRESSION AND MUTAGENESIS STUDIES OF THE BIFUNCTIONAL CATALASE-PHENOL OXIDASE FROM SCYTALIDIUM THERMOPHILUM

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY. DISORDERED REGION BETWEEN RESIDUE 617 AND 622 IN CHAIN A WAS NOT MODELED DUE TO WEAK DENSITY. C-TERMINAL RESIDUE SER698 IN CHAIN A WAS NOT MODELED DUE TO WEAK DENSITY. DISORDERED REGION BETWEEN RESIDUE 617 AND 622 IN CHAIN B WAS NOT MODELED DUE TO WEAK DENSITY. DISORDERED REGION BETWEEN RESIDUE 618 AND 622 IN CHAIN C WAS NOT MODELED DUE TO WEAK DENSITY. DISORDERED REGION BETWEEN RESIDUE 649 AND 653 IN CHAIN C WAS NOT MODELED DUE TO WEAK DENSITY. C-TERMINAL RESIDUE SER698 IN CHAIN C WAS NOT MODELED DUE TO WEAK DENSITY. DISORDERED REGION BETWEEN RESIDUE 618 AND 622 IN CHAIN D WAS NOT MODELED DUE TO WEAK DENSITY. DISORDERED REGION BETWEEN RESIDUE 649 AND 654 IN CHAIN D WAS NOT MODELED DUE TO WEAK DENSITY. C-TERMINAL RESIDUE SER698 IN CHAIN D WAS NOT MODELED DUE TO WEAK DENSITY. RESIDUE GLU654 IN CHAIN D HAVING B FACTOR VALUE GREATER THAN 100 PRESENT ON THE SURFACE WAS MODELED FROM POOR DENSITY MAP. WATER MOLECULES F1198 AND F1441 PRESENT NEXT TO ARG127 IN CHAIN A HAVE OCCUPANCY VALUES OF 0.5. WATER MOLECULES F1076 AND F1159 PRESENT NEXT TO ARG127 IN CHAIN B HAVE OCCUPANCY VALUES OF 0.5. WATER MOLECULES F1133, F1252 AND F1278 PRESENT NEXT TO ARG127 IN CHAIN C HAVE OCCUPANCY VALUES OF 0.5. WATER MOLECULES F1071 AND F1428 PRESENT NEXT TO ARG127 IN CHAIN D HAVE OCCUPANCY VALUES OF 0.5. WATER MOLECULES F894, F1057, F1059, F1072 AND F1073 WERE PLACED SO THAT THE COMPLEXES FORMED WERE FIVE COORDINATE FOR CA1.
OXIDOREDUCTASE, HEME CATALASE, MOLECULAR CHANNELS, OXIDATIVE ACTIVITY