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 | arginine catabolic process |
A | 0008295 | biological_process | spermidine biosynthetic process |
A | 0008792 | molecular_function | arginine decarboxylase activity |
A | 0009446 | biological_process | putrescine biosynthetic process |
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 | arginine catabolic process |
B | 0008295 | biological_process | spermidine biosynthetic process |
B | 0008792 | molecular_function | arginine decarboxylase activity |
B | 0009446 | biological_process | putrescine biosynthetic process |
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 | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | PHE307 | |
B | PHE307 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS127 | |
B | LYS127 |