3NZQ
Crystal Structure of Biosynthetic arginine decarboxylase ADC (SpeA) from Escherichia coli, Northeast Structural Genomics Consortium Target ER600
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0008792 | molecular_function | arginine decarboxylase activity |
| A | 0009446 | biological_process | putrescine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0008792 | molecular_function | arginine decarboxylase activity |
| B | 0009446 | biological_process | putrescine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 701 |
| Chain | Residue |
| A | VAL128 |
| A | SER275 |
| A | GLY312 |
| A | LEU313 |
| A | GLY362 |
| A | ARG363 |
| A | TYR568 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | HOH672 |
| A | HIS429 |
| A | HIS432 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 701 |
| Chain | Residue |
| B | VAL128 |
| B | SER275 |
| B | GLY312 |
| B | LEU313 |
| B | GLU360 |
| B | GLY362 |
| B | ARG363 |
| B | TYR568 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 702 |
| Chain | Residue |
| B | TRP233 |
| B | HIS429 |
| B | HIS432 |
| B | HOH673 |
| B | HOH704 |
Functional Information from PROSITE/UniProt
| site_id | PS00878 |
| Number of Residues | 19 |
| Details | ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YPiKVNqhrrVIesLihsG |
| Chain | Residue | Details |
| A | TYR124-GLY142 |
| site_id | PS00879 |
| Number of Residues | 14 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gvn....IqCFDVGGGLG |
| Chain | Residue | Details |
| A | GLY301-GLY314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
