3MBO
Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0071793 | biological_process | bacillithiol biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0071793 | biological_process | bacillithiol biosynthetic process |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0071793 | biological_process | bacillithiol biosynthetic process |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0071793 | biological_process | bacillithiol biosynthetic process |
E | 0000166 | molecular_function | nucleotide binding |
E | 0016757 | molecular_function | glycosyltransferase activity |
E | 0071793 | biological_process | bacillithiol biosynthetic process |
F | 0000166 | molecular_function | nucleotide binding |
F | 0016757 | molecular_function | glycosyltransferase activity |
F | 0071793 | biological_process | bacillithiol biosynthetic process |
G | 0000166 | molecular_function | nucleotide binding |
G | 0016757 | molecular_function | glycosyltransferase activity |
G | 0071793 | biological_process | bacillithiol biosynthetic process |
H | 0000166 | molecular_function | nucleotide binding |
H | 0016757 | molecular_function | glycosyltransferase activity |
H | 0071793 | biological_process | bacillithiol biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE UDP A 382 |
Chain | Residue |
A | VAL13 |
A | GLY285 |
A | LEU286 |
A | GLU290 |
A | GOL386 |
A | GLY14 |
A | GLY15 |
A | ILE204 |
A | ASN206 |
A | LYS211 |
A | VAL234 |
A | GLN262 |
A | GLU282 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE UDP C 382 |
Chain | Residue |
C | GLY15 |
C | ILE204 |
C | LYS211 |
C | LYS261 |
C | GLN262 |
C | GLU282 |
C | GLY285 |
C | LEU286 |
C | VAL287 |
C | GLU290 |
C | GOL383 |
C | MLT385 |
C | MG386 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE UDP H 382 |
Chain | Residue |
H | GLY15 |
H | ILE204 |
H | SER205 |
H | ASN206 |
H | GLY235 |
H | ASP236 |
H | LEU286 |
H | GLU290 |
H | MLT384 |
H | HOH427 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UDP E 382 |
Chain | Residue |
E | GLY15 |
E | ILE204 |
E | SER205 |
E | ASN206 |
E | LYS211 |
E | GLN262 |
E | ASP263 |
E | ASN264 |
E | VAL265 |
E | GLY285 |
E | LEU286 |
E | GLU290 |
E | GOL384 |
E | MLT387 |
E | MG388 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 383 |
Chain | Residue |
A | ARG138 |
A | GLU142 |
A | LYS163 |
A | ASN165 |
D | ASN165 |
D | ASP167 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL F 382 |
Chain | Residue |
F | LYS182 |
F | ARG183 |
F | LEU269 |
F | ALA270 |
F | SER272 |
F | CYS294 |
F | GLY295 |
F | VAL296 |
F | HIS341 |
F | HOH399 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL F 383 |
Chain | Residue |
F | ASN46 |
F | LYS47 |
F | TYR49 |
F | ILE52 |
F | PHE54 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL E 383 |
Chain | Residue |
E | GLY313 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL F 384 |
Chain | Residue |
E | TYR67 |
E | PRO68 |
F | PRO68 |
F | TYR70 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 382 |
Chain | Residue |
D | VAL59 |
D | ASN60 |
D | VAL64 |
D | GLN66 |
D | PRO69 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL H 383 |
Chain | Residue |
H | LYS2 |
H | TYR370 |
H | ARG374 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 384 |
Chain | Residue |
A | THR367 |
A | TYR370 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 382 |
Chain | Residue |
B | THR125 |
B | SER153 |
B | GLU157 |
B | LYS281 |
B | GLU282 |
B | GLY304 |
B | GOL383 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL D 383 |
Chain | Residue |
D | ALA221 |
D | THR225 |
D | LEU250 |
D | HIS251 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 384 |
Chain | Residue |
D | HIS251 |
D | ASN249 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 385 |
Chain | Residue |
A | GLN169 |
A | THR170 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 386 |
Chain | Residue |
A | GLY121 |
A | THR122 |
A | THR125 |
A | GLU282 |
A | SER283 |
A | UDP382 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 383 |
Chain | Residue |
B | GLU157 |
B | GOL382 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 384 |
Chain | Residue |
E | VAL179 |
E | TYR180 |
E | ASN264 |
E | VAL265 |
E | ALA266 |
E | GLU290 |
E | UDP382 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 383 |
Chain | Residue |
C | PHE43 |
C | TYR180 |
C | VAL265 |
C | GLU290 |
C | UDP382 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 387 |
Chain | Residue |
A | GLU354 |
A | GLN355 |
A | LYS360 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL E 385 |
Chain | Residue |
E | LYS182 |
E | CYS294 |
E | GLY295 |
E | GLY345 |
E | ARG349 |
G | ASP236 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 384 |
Chain | Residue |
C | SER363 |
C | GLN364 |
C | THR367 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL F 385 |
Chain | Residue |
F | GLY121 |
F | GLU282 |
F | SER283 |
F | PHE284 |
F | GLY285 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL E 386 |
Chain | Residue |
E | ASP145 |
E | VAL146 |
E | VAL147 |
E | LYS166 |
E | ASP167 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MLT H 384 |
Chain | Residue |
H | GLY14 |
H | GLY15 |
H | SER16 |
H | TYR94 |
H | THR122 |
H | ASN206 |
H | UDP382 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MLT A 388 |
Chain | Residue |
A | TYR10 |
A | SER16 |
A | TYR94 |
A | THR122 |
B | VAL64 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MLT C 385 |
Chain | Residue |
C | VAL13 |
C | GLY14 |
C | GLY15 |
C | SER16 |
C | TYR94 |
C | THR122 |
C | UDP382 |
C | HOH397 |
site_id | DC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MLT E 387 |
Chain | Residue |
E | GLY14 |
E | GLY15 |
E | SER16 |
E | THR122 |
E | ASN206 |
E | UDP382 |
F | PHE65 |
site_id | DC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 386 |
Chain | Residue |
C | GLU282 |
C | GLY285 |
C | UDP382 |
site_id | DC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 388 |
Chain | Residue |
E | GLU282 |
E | PHE284 |
E | UDP382 |
E | HOH400 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20799687, ECO:0007744|PDB:3MBO |
Chain | Residue | Details |
A | SER16 | |
B | ASN206 | |
B | GLN262 | |
B | GLU290 | |
C | SER16 | |
C | TYR94 | |
C | THR122 | |
C | ASN206 | |
C | GLN262 | |
C | GLU290 | |
D | SER16 | |
A | TYR94 | |
D | TYR94 | |
D | THR122 | |
D | ASN206 | |
D | GLN262 | |
D | GLU290 | |
E | SER16 | |
E | TYR94 | |
E | THR122 | |
E | ASN206 | |
E | GLN262 | |
A | THR122 | |
E | GLU290 | |
F | SER16 | |
F | TYR94 | |
F | THR122 | |
F | ASN206 | |
F | GLN262 | |
F | GLU290 | |
G | SER16 | |
G | TYR94 | |
G | THR122 | |
A | ASN206 | |
G | ASN206 | |
G | GLN262 | |
G | GLU290 | |
H | SER16 | |
H | TYR94 | |
H | THR122 | |
H | ASN206 | |
H | GLN262 | |
H | GLU290 | |
A | GLN262 | |
A | GLU290 | |
B | SER16 | |
B | TYR94 | |
B | THR122 |