1HV9
STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
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 | 0005829 | cellular_component | cytosol |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000902 | biological_process | cell morphogenesis |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 9027 |
| Chain | Residue |
| B | LYS25 |
| B | ASP105 |
| B | ASN227 |
| B | UD13002 |
| B | HOH5026 |
| B | HOH5027 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO B 9028 |
| Chain | Residue |
| B | HOH5045 |
| B | HOH5045 |
| B | HOH5045 |
| B | CO9029 |
| B | CO9029 |
| B | CO9029 |
| B | ASP406 |
| B | ASP406 |
| B | ASP406 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO B 9029 |
| Chain | Residue |
| B | ASP406 |
| B | ASP406 |
| B | ASP406 |
| B | HOH6868 |
| B | HOH6868 |
| B | HOH6868 |
| B | CO9028 |
| B | CO9028 |
| B | CO9028 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO A 9030 |
| Chain | Residue |
| A | ASP406 |
| A | ASP406 |
| A | ASP406 |
| A | HOH6867 |
| A | HOH6867 |
| A | HOH6867 |
| A | CO9031 |
| A | CO9031 |
| A | CO9031 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO A 9031 |
| Chain | Residue |
| A | ASP406 |
| A | ASP406 |
| A | ASP406 |
| A | HOH6036 |
| A | HOH6036 |
| A | HOH6036 |
| A | CO9030 |
| A | CO9030 |
| A | CO9030 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COA A 2001 |
| Chain | Residue |
| A | CYS385 |
| A | TYR387 |
| A | SER405 |
| A | ALA422 |
| A | ALA423 |
| A | ARG440 |
| A | LYS446 |
| A | HOH4037 |
| A | HOH5142 |
| A | HOH5458 |
| B | ARG429 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE COA B 2002 |
| Chain | Residue |
| A | ARG429 |
| B | CYS385 |
| B | TYR387 |
| B | GLY404 |
| B | SER405 |
| B | ALA422 |
| B | ALA423 |
| B | ARG440 |
| B | LYS446 |
| B | TRP449 |
| B | HOH4051 |
| B | HOH5166 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UD1 A 3001 |
| Chain | Residue |
| A | LEU11 |
| A | ALA13 |
| A | GLY14 |
| A | GLN76 |
| A | GLN79 |
| A | LEU80 |
| A | GLY81 |
| A | THR82 |
| A | TYR103 |
| A | ASP105 |
| A | GLY140 |
| A | GLU154 |
| A | ASN169 |
| A | THR170 |
| A | TYR197 |
| A | ILE198 |
| A | THR199 |
| A | HOH5272 |
| A | HOH5373 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UD1 B 3002 |
| Chain | Residue |
| B | ASN169 |
| B | THR199 |
| B | ASN227 |
| B | HOH5006 |
| B | HOH5026 |
| B | HOH5027 |
| B | HOH5120 |
| B | HOH5264 |
| B | CO9027 |
| B | LEU11 |
| B | ALA12 |
| B | ALA13 |
| B | GLY14 |
| B | LYS25 |
| B | GLN76 |
| B | GLN79 |
| B | GLY81 |
| B | THR82 |
| B | TYR103 |
| B | GLY104 |
| B | ASP105 |
| B | TYR139 |
| B | GLY140 |
| B | GLU154 |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVtVGkgAtIAagTtVtrnV |
| Chain | Residue | Details |
| A | VAL403-VAL431 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | HIS363 | |
| B | HIS363 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010 |
| Chain | Residue | Details |
| A | LEU11 | |
| B | GLY81 | |
| B | TYR103 | |
| B | GLY140 | |
| B | GLU154 | |
| B | ASN169 | |
| A | GLN76 | |
| A | GLY81 | |
| A | TYR103 | |
| A | GLY140 | |
| A | GLU154 | |
| A | ASN169 | |
| B | LEU11 | |
| B | GLN76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | LYS25 | |
| A | ASN227 | |
| A | ASN386 | |
| B | LYS25 | |
| B | ASN227 | |
| B | ASN386 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17473010, ECO:0007744|PDB:2OI5 |
| Chain | Residue | Details |
| A | ASP105 | |
| B | ASP105 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010 |
| Chain | Residue | Details |
| A | ARG333 | |
| A | LYS351 | |
| A | TYR366 | |
| B | ARG333 | |
| B | LYS351 | |
| B | TYR366 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832 |
| Chain | Residue | Details |
| A | ASN377 | |
| A | SER405 | |
| A | ALA423 | |
| A | ARG440 | |
| B | ASN377 | |
| B | SER405 | |
| B | ALA423 | |
| B | ARG440 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832 |
| Chain | Residue | Details |
| A | ALA380 | |
| B | ALA380 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 10428949 |
| Chain | Residue | Details |
| A | ARG18 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 10428949 |
| Chain | Residue | Details |
| B | ARG18 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| A | ARG18 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| B | ARG18 | electrostatic stabiliser |
