6DLI
Crystal structure of glutamate racemase from Thermus thermophilus in complex with Beta-chloro-D-alanine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008881 | molecular_function | glutamate racemase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
A | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
A | 0071555 | biological_process | cell wall organization |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008881 | molecular_function | glutamate racemase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
B | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
B | 0071555 | biological_process | cell wall organization |
C | 0008360 | biological_process | regulation of cell shape |
C | 0008881 | molecular_function | glutamate racemase activity |
C | 0009252 | biological_process | peptidoglycan biosynthetic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
C | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
C | 0071555 | biological_process | cell wall organization |
D | 0008360 | biological_process | regulation of cell shape |
D | 0008881 | molecular_function | glutamate racemase activity |
D | 0009252 | biological_process | peptidoglycan biosynthetic process |
D | 0016853 | molecular_function | isomerase activity |
D | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
D | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue C2N A 301 |
Chain | Residue |
A | ASP12 |
A | SER13 |
A | CYS75 |
A | ASN76 |
A | THR77 |
A | THR116 |
A | CYS176 |
A | THR177 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | TYR128 |
A | ASP130 |
A | ARG106 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue C2N B 301 |
Chain | Residue |
B | ASP12 |
B | SER13 |
B | TYR44 |
B | CYS75 |
B | ASN76 |
B | THR77 |
B | THR116 |
B | CYS176 |
B | THR177 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue C2N C 301 |
Chain | Residue |
C | ASP12 |
C | SER13 |
C | PRO43 |
C | TYR44 |
C | GLY45 |
C | CYS75 |
C | ASN76 |
C | THR77 |
C | THR116 |
C | THR177 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue GOL C 302 |
Chain | Residue |
C | VAL68 |
C | VAL92 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue C2N D 301 |
Chain | Residue |
D | ASP12 |
D | SER13 |
D | CYS75 |
D | ASN76 |
D | THR77 |
D | THR116 |
D | CYS176 |
D | THR177 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue GOL D 302 |
Chain | Residue |
D | VAL68 |
D | VAL92 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00258 |
Chain | Residue | Details |
A | CYS75 | |
A | CYS176 | |
B | CYS75 | |
B | CYS176 | |
C | CYS75 | |
C | CYS176 | |
D | CYS75 | |
D | CYS176 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258 |
Chain | Residue | Details |
A | ASP12 | |
C | TYR44 | |
C | ASN76 | |
C | THR177 | |
D | ASP12 | |
D | TYR44 | |
D | ASN76 | |
D | THR177 | |
A | TYR44 | |
A | ASN76 | |
A | THR177 | |
B | ASP12 | |
B | TYR44 | |
B | ASN76 | |
B | THR177 | |
C | ASP12 |