3SPT
Crystal structure of GlmU from Mycobacterium tuberculosis in complex with ACETYL COENZYME A and URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0035635 | biological_process | entry of bacterium into host cell |
| A | 0044650 | biological_process | adhesion of symbiont to host cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070569 | molecular_function | uridylyltransferase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 497 |
| Chain | Residue |
| A | ASP114 |
| A | ASN239 |
| A | UD1498 |
| A | HOH711 |
| A | HOH712 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 499 |
| Chain | Residue |
| A | HOH501 |
| A | HOH501 |
| A | HOH501 |
| A | SER392 |
| A | ASP417 |
| A | ASP417 |
| A | ASP417 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ACO A 496 |
| Chain | Residue |
| A | GLY390 |
| A | ALA391 |
| A | VAL394 |
| A | VAL396 |
| A | ASN397 |
| A | TYR398 |
| A | THR414 |
| A | GLY415 |
| A | SER416 |
| A | GLY433 |
| A | ALA434 |
| A | ARG439 |
| A | VAL449 |
| A | ALA451 |
| A | ARG455 |
| A | ILE457 |
| A | TRP460 |
| A | LYS464 |
| A | ARG465 |
| A | HOH516 |
| A | HOH592 |
| A | HOH632 |
| A | HOH652 |
| A | HOH694 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UD1 A 498 |
| Chain | Residue |
| A | LEU12 |
| A | ALA13 |
| A | ALA14 |
| A | GLY15 |
| A | ARG19 |
| A | GLN83 |
| A | PRO86 |
| A | LEU87 |
| A | GLY88 |
| A | THR89 |
| A | ALA92 |
| A | ASP114 |
| A | TYR150 |
| A | GLY151 |
| A | GLU166 |
| A | ASN181 |
| A | TYR209 |
| A | THR211 |
| A | ASN239 |
| A | MG497 |
| A | HOH527 |
| A | HOH596 |
| A | HOH704 |
| A | HOH711 |
| A | HOH712 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305|Ref.7 |
| Chain | Residue | Details |
| A | HIS374 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | LEU12 | |
| A | GLY88 | |
| A | GLY151 | |
| A | GLU166 | |
| A | ASN181 | |
| A | ASN239 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | LYS26 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | GLN83 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:19237750, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | SER112 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19121323, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.7, ECO:0007744|PDB:3SPT, ECO:0007744|PDB:4HCQ |
| Chain | Residue | Details |
| A | ASP114 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:23485416, ECO:0000269|Ref.8 |
| Chain | Residue | Details |
| A | ARG344 | |
| A | LYS362 | |
| A | TYR377 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | ASN388 | |
| A | ALA391 | |
| A | SER416 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | ASN397 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | ALA434 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609 |
| Chain | Residue | Details |
| A | THR2 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036 |
| Chain | Residue | Details |
| A | LYS362 |
