4G3Q
Crystal structure of GlmU from Mycobacterium tuberculosis Snapshot 4
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 | 15 |
Details | BINDING SITE FOR RESIDUE POP A 501 |
Chain | Residue |
A | PRO16 |
A | HOH1133 |
A | HOH1134 |
A | HOH1135 |
A | HOH1136 |
A | HOH1143 |
A | HOH1144 |
A | GLY17 |
A | THR18 |
A | ARG19 |
A | MG502 |
A | UD1506 |
A | HOH601 |
A | HOH1033 |
A | HOH1132 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | POP501 |
A | HOH1132 |
A | HOH1133 |
A | HOH1134 |
A | HOH1135 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | ASP417 |
A | ASP417 |
A | ASP417 |
A | CO505 |
A | CO505 |
A | CO505 |
A | HOH602 |
A | HOH602 |
A | HOH602 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO A 504 |
Chain | Residue |
A | ASP114 |
A | ASN239 |
A | UD1506 |
A | HOH1137 |
A | HOH1138 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO A 505 |
Chain | Residue |
A | ASP417 |
A | ASP417 |
A | ASP417 |
A | MG503 |
A | MG503 |
A | MG503 |
site_id | AC6 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE UD1 A 506 |
Chain | Residue |
A | LEU12 |
A | ALA13 |
A | ALA14 |
A | GLY15 |
A | ARG19 |
A | LYS26 |
A | GLN83 |
A | PRO86 |
A | LEU87 |
A | GLY88 |
A | THR89 |
A | ALA92 |
A | SER112 |
A | GLY113 |
A | ASP114 |
A | TYR150 |
A | GLY151 |
A | GLU166 |
A | ASN181 |
A | ALA182 |
A | TYR209 |
A | THR211 |
A | ASN239 |
A | POP501 |
A | CO504 |
A | HOH624 |
A | HOH643 |
A | HOH670 |
A | HOH791 |
A | HOH1034 |
A | HOH1036 |
A | HOH1133 |
A | HOH1137 |
A | HOH1138 |
A | HOH1143 |
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 | GLY151 | |
A | GLU166 | |
A | ASN181 | |
A | ASN239 | |
A | LEU12 | |
A | GLY88 |
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 | LYS362 | |
A | TYR377 | |
A | ARG344 |
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 | ALA391 | |
A | SER416 | |
A | ASN388 |
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 |