4IMD
Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase trapped with pyruvate covalently bound through a Schiff base to Lys164
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0019262 | biological_process | N-acetylneuraminate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 301 |
Chain | Residue |
A | ALA179 |
A | TYR180 |
A | PRO181 |
A | ASN182 |
A | HIS183 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | ASN182 |
A | HOH577 |
A | HOH579 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | GLU191 |
A | HOH580 |
A | HOH593 |
A | ASP190 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | GLY226 |
A | LEU228 |
A | LYS229 |
A | HOH581 |
B | GLN224 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | LYS2 |
A | TYR132 |
A | HOH522 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 301 |
Chain | Residue |
B | ALA179 |
B | TYR180 |
B | PRO181 |
B | ASN182 |
B | HIS183 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | ASP190 |
B | GLU191 |
B | HOH568 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | LEU161 |
B | ASN182 |
B | HOH524 |
B | HOH600 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 301 |
Chain | Residue |
C | TYR180 |
C | PRO181 |
C | ASN182 |
C | HIS183 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 302 |
Chain | Residue |
C | THR107 |
C | SER137 |
C | ILE138 |
C | PRO139 |
C | THR142 |
C | VAL144 |
C | ILE146 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 303 |
Chain | Residue |
C | PHE189 |
C | ASP190 |
C | GLU191 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 D 301 |
Chain | Residue |
D | TYR180 |
D | PRO181 |
D | ASN182 |
D | HIS183 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 302 |
Chain | Residue |
D | THR107 |
D | TYR136 |
D | SER137 |
D | ILE138 |
D | PRO139 |
D | THR142 |
D | VAL144 |
D | ILE146 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 303 |
Chain | Residue |
D | ASP190 |
D | GLU191 |
D | HOH565 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO D 304 |
Chain | Residue |
D | LEU161 |
D | ASN182 |
Functional Information from PROSITE/UniProt
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VdGLYvGGstgenfmLstEekkeifR |
Chain | Residue | Details |
A | VAL39-ARG64 |
site_id | PS00665 |
Number of Residues | 18 |
Details | DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGENfmlsteE |
Chain | Residue | Details |
A | GLY41-GLU58 |
site_id | PS00666 |
Number of Residues | 31 |
Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YSIPflTgvnIgveqfgelyknpk.VlGVKFT |
Chain | Residue | Details |
A | TYR136-THR166 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237 |
Chain | Residue | Details |
A | TYR136 | |
B | TYR136 | |
C | TYR136 | |
D | TYR136 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:24152047 |
Chain | Residue | Details |
A | KPI164 | |
B | KPI164 | |
C | KPI164 | |
D | KPI164 |
site_id | SWS_FT_FI3 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24152047, ECO:0007744|PDB:4IMF |
Chain | Residue | Details |
A | SER47 | |
B | SER47 | |
B | THR48 | |
B | TYR136 | |
B | THR166 | |
B | GLY188 | |
B | ASP190 | |
B | GLU191 | |
B | SER207 | |
B | TYR251 | |
C | SER47 | |
A | THR48 | |
C | THR48 | |
C | TYR136 | |
C | THR166 | |
C | GLY188 | |
C | ASP190 | |
C | GLU191 | |
C | SER207 | |
C | TYR251 | |
D | SER47 | |
D | THR48 | |
A | TYR136 | |
D | TYR136 | |
D | THR166 | |
D | GLY188 | |
D | ASP190 | |
D | GLU191 | |
D | SER207 | |
D | TYR251 | |
A | THR166 | |
A | GLY188 | |
A | ASP190 | |
A | GLU191 | |
A | SER207 | |
A | TYR251 |