2EHU
Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and Inhibitor L-serine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
A | 0010133 | biological_process | proline catabolic process to glutamate |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
B | 0010133 | biological_process | proline catabolic process to glutamate |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 1540 |
Chain | Residue |
A | SER55 |
A | LEU56 |
A | GLU123 |
A | ASP211 |
A | HOH2729 |
A | HOH2809 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 1519 |
Chain | Residue |
A | ALA271 |
A | NAD1518 |
A | HOH2892 |
A | ALA245 |
A | GLU249 |
A | ILE268 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 1520 |
Chain | Residue |
A | ARG462 |
A | PHE464 |
A | HIS465 |
A | HOH2674 |
B | LYS510 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 2519 |
Chain | Residue |
B | ALA245 |
B | GLU249 |
B | ILE268 |
B | ALA271 |
B | NAD2518 |
B | HOH2901 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 2520 |
Chain | Residue |
A | LYS510 |
B | ARG462 |
B | PHE464 |
B | HIS465 |
B | HOH2734 |
B | HOH2982 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 2540 |
Chain | Residue |
B | SER55 |
B | LEU56 |
B | GLU123 |
B | ASP211 |
B | HOH2794 |
B | HOH2907 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SER A 1517 |
Chain | Residue |
A | PHE185 |
A | CYS322 |
A | SER323 |
A | GLY477 |
A | ALA478 |
A | PHE485 |
A | HOH2539 |
A | HOH2633 |
A | HOH2890 |
A | HOH3024 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAD A 1518 |
Chain | Residue |
A | ILE180 |
A | ALA181 |
A | PRO182 |
A | TRP183 |
A | ASN184 |
A | ILE189 |
A | LYS207 |
A | ALA209 |
A | GLU210 |
A | GLY240 |
A | GLY244 |
A | ALA245 |
A | PHE258 |
A | THR259 |
A | GLY260 |
A | SER261 |
A | VAL264 |
A | GLU288 |
A | THR289 |
A | GLY290 |
A | CYS322 |
A | GLU417 |
A | PHE419 |
A | PHE485 |
A | ACT1519 |
A | HOH2641 |
A | HOH2719 |
A | HOH2814 |
A | HOH2865 |
A | HOH2881 |
A | HOH2919 |
A | HOH2923 |
A | HOH2955 |
A | HOH3024 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SER B 2517 |
Chain | Residue |
B | PHE185 |
B | CYS322 |
B | SER323 |
B | GLY477 |
B | ALA478 |
B | PHE485 |
B | HOH2551 |
B | HOH2664 |
B | HOH2896 |
B | HOH3038 |
site_id | BC1 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAD B 2518 |
Chain | Residue |
B | GLY244 |
B | ALA245 |
B | PHE258 |
B | THR259 |
B | GLY260 |
B | SER261 |
B | VAL264 |
B | GLU288 |
B | THR289 |
B | GLY290 |
B | CYS322 |
B | GLU417 |
B | PHE419 |
B | LEU445 |
B | PHE485 |
B | ACT2519 |
B | HOH2647 |
B | HOH2713 |
B | HOH2788 |
B | HOH2871 |
B | HOH2905 |
B | HOH2977 |
B | HOH3038 |
B | ILE180 |
B | ALA181 |
B | PRO182 |
B | TRP183 |
B | ASN184 |
B | ILE189 |
B | LYS207 |
B | ALA209 |
B | GLU210 |
B | GLY240 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MPD A 1531 |
Chain | Residue |
A | ASP359 |
A | HOH2681 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 1532 |
Chain | Residue |
A | PHE6 |
A | TYR144 |
A | ALA148 |
A | HOH2585 |
A | HOH2602 |
A | HOH2714 |
A | HOH2981 |
B | GLU158 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 1533 |
Chain | Residue |
A | PHE170 |
A | HOH3006 |
B | PRO94 |
B | ARG462 |
B | HOH2694 |
B | HOH2933 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MPD A 1534 |
Chain | Residue |
A | ARG36 |
A | PRO39 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 1535 |
Chain | Residue |
A | GLN279 |
A | HOH2648 |
A | HOH2941 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 2531 |
Chain | Residue |
A | HOH3007 |
B | ARG151 |
B | TYR171 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD B 2532 |
Chain | Residue |
A | GLU158 |
B | PHE6 |
B | TYR144 |
B | ALA148 |
B | HOH2593 |
B | HOH2597 |
B | HOH2718 |
B | HOH2921 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 2533 |
Chain | Residue |
A | PRO94 |
A | ARG462 |
A | HOH2782 |
B | TYR154 |
B | PHE170 |
B | HOH2819 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 2534 |
Chain | Residue |
A | ARG151 |
A | TYR171 |
A | HOH2820 |
A | HOH3007 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD B 2535 |
Chain | Residue |
A | LEU27 |
A | ARG28 |
A | TYR122 |
A | GLU355 |
B | PRO353 |
B | GLU355 |
B | GLU356 |
B | HOH2671 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD B 2536 |
Chain | Residue |
B | LEU275 |
B | GLN279 |
B | HOH2638 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD B 2537 |
Chain | Residue |
B | ARG36 |
B | GLU221 |
B | HOH2659 |
B | HOH2886 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD B 2538 |
Chain | Residue |
B | TYR315 |
B | GLY316 |
B | ASP359 |
B | HOH2686 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgFQGQKCSAAS |
Chain | Residue | Details |
A | TYR315-SER326 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGKDA |
Chain | Residue | Details |
A | VAL287-ALA294 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | CYS322 | |
A | ASN184 | |
A | GLU288 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | CYS322 | |
B | ASN184 | |
B | GLU288 |