2GR9
Crystal structure of P5CR complexed with NADH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
A | 0006561 | biological_process | proline biosynthetic process |
B | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
B | 0006561 | biological_process | proline biosynthetic process |
C | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
C | 0006561 | biological_process | proline biosynthetic process |
D | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
D | 0006561 | biological_process | proline biosynthetic process |
E | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
E | 0006561 | biological_process | proline biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NAI A 1300 |
Chain | Residue |
A | ARG129 |
A | HOH1412 |
A | HOH1431 |
A | HOH1435 |
C | ARG204 |
C | GLN208 |
C | HOH3395 |
A | GLU130 |
A | SER154 |
A | GLY157 |
A | PHE158 |
A | LEU218 |
A | HIS219 |
A | GLU1301 |
A | HOH1408 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GLU A 1301 |
Chain | Residue |
A | NAI1300 |
A | HOH1401 |
A | HOH1408 |
A | HOH1429 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAI B 2300 |
Chain | Residue |
B | ARG129 |
B | GLU130 |
B | SER154 |
B | SER155 |
B | VAL156 |
B | GLY157 |
B | PHE158 |
B | ARG200 |
B | ARG204 |
B | GLN208 |
B | LEU211 |
B | LEU218 |
B | HIS219 |
B | GLU2301 |
B | HOH2359 |
B | HOH2377 |
B | HOH2380 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GLU B 2301 |
Chain | Residue |
B | ARG129 |
B | NAI2300 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAI C 3300 |
Chain | Residue |
A | ARG204 |
A | LEU205 |
A | GLN208 |
A | LEU211 |
C | ARG129 |
C | GLU130 |
C | SER154 |
C | SER155 |
C | GLY157 |
C | PHE158 |
C | LEU218 |
C | HIS219 |
C | GLU3301 |
C | HOH3408 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GLU C 3301 |
Chain | Residue |
C | ARG129 |
C | NAI3300 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAI D 4300 |
Chain | Residue |
D | GLU130 |
D | SER154 |
D | PHE158 |
D | LYS215 |
D | LEU218 |
D | HIS219 |
D | GLU4301 |
D | HOH4410 |
D | HOH4413 |
D | HOH4416 |
D | HOH4423 |
D | HOH4436 |
E | ARG204 |
E | GLN208 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GLU D 4301 |
Chain | Residue |
D | NAI4300 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NAI E 5300 |
Chain | Residue |
D | ARG204 |
D | GLN208 |
E | GLU130 |
E | SER154 |
E | GLY157 |
E | PHE158 |
E | LEU218 |
E | HIS219 |
E | GLU5301 |
E | HOH5402 |
E | HOH5404 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GLU E 5301 |
Chain | Residue |
E | HIS219 |
E | NAI5300 |
Functional Information from PROSITE/UniProt
site_id | PS00521 |
Number of Residues | 23 |
Details | P5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkdnVSSpGGaTihALhvLE |
Chain | Residue | Details |
A | PRO224-GLU246 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | BINDING: BINDING => ECO:0000269|Ref.18 |
Chain | Residue | Details |
A | ILE6 | |
B | CYS95 | |
C | ILE6 | |
C | SER34 | |
C | ASN56 | |
C | ALA69 | |
C | CYS95 | |
D | ILE6 | |
D | SER34 | |
D | ASN56 | |
D | ALA69 | |
A | SER34 | |
D | CYS95 | |
E | ILE6 | |
E | SER34 | |
E | ASN56 | |
E | ALA69 | |
E | CYS95 | |
A | ASN56 | |
A | ALA69 | |
A | CYS95 | |
B | ILE6 | |
B | SER34 | |
B | ASN56 | |
B | ALA69 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | MOD_RES: N-acetylserine => ECO:0000269|Ref.8, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
C | SER2 | |
D | SER2 | |
E | SER2 |