sequence The crystallized protein differs from the Swissprot sequence at residue 14. Number 14 is a ...sequence The crystallized protein differs from the Swissprot sequence at residue 14. Number 14 is a leucin, while in the Swissprot sequence number 14 is a tryptophan. This is confirmed by DNA sequencing and was also reported for the original WT structure (1qj5).
A covalent adduct is formed between pyridoxal-5'-phosphate and the amiclenomycin in the A subunit. ...A covalent adduct is formed between pyridoxal-5'-phosphate and the amiclenomycin in the A subunit. In the B subunit the density for amiclenomycin is significantly weaker. The amiclenomycin molecule is modeled as non-covalently bound in the B subunit, but the model has high B factors and is not well supported by structural data. For a better view of the pyridoxal-5'-phosphate-amiclenomycin adduct see the A subunit in the structure of the enzyme in complex with the cis-isomer (PDB ID 1mly). For details see the primary citation.
構造決定の手法: 分子置換 / 解像度: 2.15→22.36 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.923 / SU B: 9.138 / SU ML: 0.237 / 交差検証法: THROUGHOUT / σ(F): 0 / ESU R: 0.334 / ESU R Free: 0.219 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: In monomer A two stretches of residues are disordered, 159-169 and 186-192 resp. In monomer B three stretches of residues are disordered, 158-168, 189-194 and 296-301 resp. Residue 429 was ...詳細: In monomer A two stretches of residues are disordered, 159-169 and 186-192 resp. In monomer B three stretches of residues are disordered, 158-168, 189-194 and 296-301 resp. Residue 429 was excluded from both monomers. A number of sidechains on the surface of the protein are disordered. The occupancy for these is estimated to 0 in most cases.
Rfactor
反射数
%反射
Selection details
Rfree
0.24028
2108
5 %
RANDOM
Rwork
0.20465
-
-
-
all
0.207
39635
-
-
obs
0.207
39635
98.5 %
-
溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.4 Å / 溶媒モデル: BABINET MODEL WITH MASK