6UB9
Crystal structure of tryptophan synthase from M. tuberculosis - AMINOACRYLATE- AND BRD6309-BOUND FORM
Replaces: 6DUAFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0004834 | molecular_function | tryptophan synthase activity |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006568 | biological_process | tryptophan metabolic process |
A | 0016829 | molecular_function | lyase activity |
B | 0000162 | biological_process | tryptophan biosynthetic process |
B | 0004834 | molecular_function | tryptophan synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006568 | biological_process | tryptophan metabolic process |
B | 0016829 | molecular_function | lyase activity |
C | 0000162 | biological_process | tryptophan biosynthetic process |
C | 0004834 | molecular_function | tryptophan synthase activity |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006568 | biological_process | tryptophan metabolic process |
C | 0016829 | molecular_function | lyase activity |
D | 0000162 | biological_process | tryptophan biosynthetic process |
D | 0004834 | molecular_function | tryptophan synthase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006568 | biological_process | tryptophan metabolic process |
D | 0016829 | molecular_function | lyase activity |
E | 0000162 | biological_process | tryptophan biosynthetic process |
E | 0004834 | molecular_function | tryptophan synthase activity |
E | 0005829 | cellular_component | cytosol |
E | 0005886 | cellular_component | plasma membrane |
E | 0006568 | biological_process | tryptophan metabolic process |
E | 0016829 | molecular_function | lyase activity |
F | 0000162 | biological_process | tryptophan biosynthetic process |
F | 0004834 | molecular_function | tryptophan synthase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006568 | biological_process | tryptophan metabolic process |
F | 0016829 | molecular_function | lyase activity |
G | 0000162 | biological_process | tryptophan biosynthetic process |
G | 0004834 | molecular_function | tryptophan synthase activity |
G | 0005829 | cellular_component | cytosol |
G | 0005886 | cellular_component | plasma membrane |
G | 0006568 | biological_process | tryptophan metabolic process |
G | 0016829 | molecular_function | lyase activity |
H | 0000162 | biological_process | tryptophan biosynthetic process |
H | 0004834 | molecular_function | tryptophan synthase activity |
H | 0005737 | cellular_component | cytoplasm |
H | 0006568 | biological_process | tryptophan metabolic process |
H | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue FMT A 501 |
Chain | Residue |
A | GLU57 |
A | MET106 |
A | TYR181 |
A | ILE237 |
A | MLA502 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue MLA A 502 |
Chain | Residue |
A | ILE237 |
A | VAL238 |
A | GLY239 |
A | SER240 |
A | FMT501 |
A | TYR181 |
A | GLY217 |
A | LEU218 |
A | GLY219 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue FMT A 503 |
Chain | Residue |
A | GLN144 |
B | SER23 |
site_id | AC4 |
Number of Residues | 18 |
Details | binding site for residue P1T B 501 |
Chain | Residue |
B | HIS100 |
B | LYS101 |
B | THR124 |
B | GLY125 |
B | ALA126 |
B | GLY127 |
B | GLN128 |
B | HIS129 |
B | THR204 |
B | GLY246 |
B | GLY247 |
B | GLY248 |
B | SER249 |
B | ASN250 |
B | GLY317 |
B | GLU364 |
B | SER390 |
B | HOH615 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue H9V B 502 |
Chain | Residue |
A | TYR62 |
A | ASP64 |
A | GLY66 |
A | ASP136 |
B | LEU34 |
B | ILE184 |
B | ASN185 |
B | PHE188 |
B | TYR200 |
B | PHE202 |
B | PRO208 |
B | PHE211 |
B | PHE293 |
B | HIS294 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue CS B 503 |
Chain | Residue |
B | GLY246 |
B | ALA282 |
B | THR284 |
B | TYR320 |
B | GLY322 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue FMT B 504 |
Chain | Residue |
B | GLU48 |
B | ARG114 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue FMT B 505 |
Chain | Residue |
B | ARG355 |
D | LEU165 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue FMT B 506 |
Chain | Residue |
B | PRO262 |
B | ARG265 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ACT B 507 |
Chain | Residue |
B | HIS312 |
B | SER313 |
B | ASP319 |
B | HOH633 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue FMT B 508 |
Chain | Residue |
B | GLY67 |
B | ARG68 |
B | PRO69 |
D | GLY67 |
D | PRO69 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue FMT B 509 |
Chain | Residue |
B | LYS402 |
B | TRP403 |
B | HOH605 |
B | HOH621 |
H | LYS402 |
H | TRP403 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue MLA C 501 |
Chain | Residue |
C | TYR181 |
C | GLY217 |
C | GLY219 |
C | GLY239 |
C | SER240 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue FMT C 502 |
Chain | Residue |
C | GLN144 |
D | SER23 |
site_id | AD6 |
Number of Residues | 20 |
Details | binding site for residue P1T D 501 |
Chain | Residue |
D | SER390 |
D | HOH610 |
D | HIS100 |
D | LYS101 |
D | THR124 |
D | GLY125 |
D | ALA126 |
D | GLY127 |
D | GLN128 |
D | HIS129 |
D | THR204 |
D | CYS244 |
D | GLY246 |
D | GLY247 |
D | GLY248 |
D | SER249 |
D | ASN250 |
D | GLY317 |
D | LEU318 |
D | GLU364 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue H9V D 502 |
Chain | Residue |
C | TYR62 |
C | ASP64 |
C | GLY66 |
C | ASP136 |
D | VAL30 |
D | PRO31 |
D | LEU34 |
D | ILE184 |
D | PHE188 |
D | TYR200 |
D | PHE202 |
D | PRO208 |
D | PHE211 |
D | HIS294 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue CS D 503 |
Chain | Residue |
D | GLY246 |
D | ALA282 |
D | THR284 |
D | TYR320 |
D | GLY322 |
D | HOH613 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue PGE D 504 |
Chain | Residue |
D | PRO262 |
D | ARG265 |
D | GLY334 |
D | ARG335 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue FMT E 501 |
Chain | Residue |
E | ALA183 |
E | SER184 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue MLA E 502 |
Chain | Residue |
E | TYR181 |
E | GLY217 |
E | GLY219 |
E | VAL238 |
E | GLY239 |
E | SER240 |
site_id | AE3 |
Number of Residues | 19 |
Details | binding site for residue P1T F 501 |
Chain | Residue |
F | HIS100 |
F | LYS101 |
F | THR124 |
F | GLY125 |
F | ALA126 |
F | GLY127 |
F | GLN128 |
F | HIS129 |
F | THR204 |
F | GLY246 |
F | GLY247 |
F | GLY248 |
F | SER249 |
F | ASN250 |
F | GLY317 |
F | GLU364 |
F | SER390 |
F | GLY391 |
F | HOH608 |
site_id | AE4 |
Number of Residues | 12 |
Details | binding site for residue H9V F 502 |
Chain | Residue |
E | ASP64 |
E | GLY66 |
E | ASP136 |
F | VAL30 |
F | LEU34 |
F | ILE184 |
F | ASN185 |
F | PHE188 |
F | PHE202 |
F | PRO208 |
F | PHE211 |
F | HIS294 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue CS F 503 |
Chain | Residue |
F | GLY246 |
F | ALA282 |
F | THR284 |
F | TYR320 |
F | GLY322 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue MLA F 506 |
Chain | Residue |
D | ASP143 |
F | CYS137 |
F | GLY141 |
F | LEU142 |
F | GLY167 |
H | HOH601 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue PGE F 507 |
Chain | Residue |
F | PRO262 |
F | ARG265 |
F | GLY334 |
site_id | AE8 |
Number of Residues | 6 |
Details | binding site for residue MLA G 501 |
Chain | Residue |
G | TYR181 |
G | GLY217 |
G | LEU218 |
G | GLY219 |
G | GLY239 |
G | SER240 |
site_id | AE9 |
Number of Residues | 2 |
Details | binding site for residue FMT H 501 |
Chain | Residue |
F | LEU165 |
H | ARG355 |
site_id | AF1 |
Number of Residues | 18 |
Details | binding site for residue P1T H 502 |
Chain | Residue |
H | HIS100 |
H | LYS101 |
H | THR124 |
H | GLY125 |
H | ALA126 |
H | GLY127 |
H | GLN128 |
H | HIS129 |
H | THR204 |
H | GLY246 |
H | GLY247 |
H | GLY248 |
H | SER249 |
H | ASN250 |
H | GLY317 |
H | GLU364 |
H | SER390 |
H | HOH611 |
site_id | AF2 |
Number of Residues | 12 |
Details | binding site for residue H9V H 503 |
Chain | Residue |
G | ASP64 |
G | GLY66 |
G | ASP136 |
H | VAL30 |
H | LEU34 |
H | ILE184 |
H | ASN185 |
H | PHE188 |
H | PHE202 |
H | PRO208 |
H | PHE211 |
H | HIS294 |
site_id | AF3 |
Number of Residues | 5 |
Details | binding site for residue CS H 504 |
Chain | Residue |
H | GLY246 |
H | ALA282 |
H | THR284 |
H | TYR320 |
H | GLY322 |
site_id | AF4 |
Number of Residues | 3 |
Details | binding site for residue FMT H 505 |
Chain | Residue |
G | GLN144 |
H | SER23 |
H | PHE297 |
site_id | AF5 |
Number of Residues | 2 |
Details | binding site for residue EDO H 506 |
Chain | Residue |
H | ARG265 |
H | FMT507 |
site_id | AF6 |
Number of Residues | 5 |
Details | binding site for residue FMT H 507 |
Chain | Residue |
H | ARG265 |
H | LEU266 |
H | ARG335 |
H | ASP337 |
H | EDO506 |
site_id | AF7 |
Number of Residues | 2 |
Details | binding site for residue FMT H 508 |
Chain | Residue |
H | ARG119 |
H | ASN194 |
Functional Information from PROSITE/UniProt
site_id | PS00167 |
Number of Residues | 14 |
Details | TRP_SYNTHASE_ALPHA Tryptophan synthase alpha chain signature. IEVGvPYSDPGMDG |
Chain | Residue | Details |
A | ILE56-GLY69 |
site_id | PS00168 |
Number of Residues | 15 |
Details | TRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LnHtGSHKiNnvLgQ |
Chain | Residue | Details |
B | LEU94-GLN108 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00133 |
Chain | Residue | Details |
B | HIS100 | |
D | HIS100 | |
F | HIS100 | |
H | HIS100 | |
E | GLU57 | |
E | ASP68 | |
G | GLU57 | |
G | ASP68 |