3RJL
Crystal structure of 1-pyrroline-5-carboxylate dehydrogenase from Bacillus licheniformis (Target NYSGRC-000337)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0006537 | biological_process | glutamate biosynthetic process |
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 | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
B | 0006537 | biological_process | glutamate biosynthetic process |
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 |
C | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
C | 0006537 | biological_process | glutamate biosynthetic process |
C | 0010133 | biological_process | proline catabolic process to glutamate |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
D | 0006537 | biological_process | glutamate biosynthetic process |
D | 0010133 | biological_process | proline catabolic process to glutamate |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
E | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
E | 0006537 | biological_process | glutamate biosynthetic process |
E | 0010133 | biological_process | proline catabolic process to glutamate |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
F | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
F | 0006537 | biological_process | glutamate biosynthetic process |
F | 0010133 | biological_process | proline catabolic process to glutamate |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
G | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
G | 0006537 | biological_process | glutamate biosynthetic process |
G | 0010133 | biological_process | proline catabolic process to glutamate |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
H | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
H | 0006537 | biological_process | glutamate biosynthetic process |
H | 0010133 | biological_process | proline catabolic process to glutamate |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 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 | 4 |
Details | BINDING SITE FOR RESIDUE CD A 539 |
Chain | Residue |
A | GLU343 |
A | HOH557 |
A | HOH587 |
B | GLU343 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD A 540 |
Chain | Residue |
A | ASP393 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 541 |
Chain | Residue |
A | GLU352 |
A | HOH803 |
B | GLU16 |
B | HOH802 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 542 |
Chain | Residue |
A | SER429 |
A | GLU433 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CD A 543 |
Chain | Residue |
A | ASP432 |
A | HOH634 |
A | HOH635 |
A | HOH636 |
D | ASP455 |
D | CD539 |
D | ACT544 |
D | HOH797 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 544 |
Chain | Residue |
A | ASP455 |
D | GLU436 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD A 545 |
Chain | Residue |
A | GLU224 |
A | ACT548 |
D | LYS108 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 546 |
Chain | Residue |
A | ASP94 |
A | GLU96 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 547 |
Chain | Residue |
A | GLU298 |
D | ASP299 |
D | ASN453 |
D | HIS456 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 548 |
Chain | Residue |
A | LYS108 |
A | ARG111 |
A | GLU224 |
A | CD545 |
D | GLU224 |
D | HOH799 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD B 539 |
Chain | Residue |
B | LYS108 |
B | GLU224 |
B | ACT543 |
B | HOH638 |
B | HOH639 |
B | HOH801 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 540 |
Chain | Residue |
B | GLU352 |
B | HOH662 |
B | HOH663 |
B | HOH664 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 541 |
Chain | Residue |
B | ASP297 |
B | GLU298 |
B | HIS456 |
C | GLU298 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 542 |
Chain | Residue |
B | GLU400 |
B | HOH659 |
B | HOH660 |
B | HOH661 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 543 |
Chain | Residue |
B | LYS108 |
B | GLU224 |
B | CD539 |
B | HOH801 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD C 539 |
Chain | Residue |
B | LYS108 |
B | HOH800 |
C | GLU224 |
C | HOH678 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD C 540 |
Chain | Residue |
C | GLU343 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD C 541 |
Chain | Residue |
C | GLU433 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD C 542 |
Chain | Residue |
C | GLU23 |
C | HOH677 |
C | HOH812 |
D | GLU16 |
D | CD543 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD C 543 |
Chain | Residue |
C | ASP74 |
G | ASP74 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD C 544 |
Chain | Residue |
C | ASP94 |
C | GLU96 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD C 545 |
Chain | Residue |
C | GLU162 |
C | HOH825 |
C | HOH826 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD C 546 |
Chain | Residue |
C | ASP374 |
C | HOH827 |
C | HOH828 |
C | HOH829 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD C 547 |
Chain | Residue |
C | ASP432 |
C | CD549 |
C | HOH813 |
C | HOH814 |
C | HOH816 |
C | HOH830 |
site_id | CC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD C 548 |
Chain | Residue |
B | GLU436 |
C | ASP455 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD C 549 |
Chain | Residue |
B | ASP432 |
C | HIS456 |
C | CD547 |
C | HOH816 |
C | HOH817 |
C | HOH818 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD D 539 |
Chain | Residue |
A | HIS456 |
A | CD543 |
D | ASP432 |
D | ACT544 |
D | HOH797 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD D 540 |
Chain | Residue |
D | GLU224 |
D | HOH716 |
D | HOH718 |
D | HOH798 |
D | HOH799 |
site_id | DC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD D 541 |
Chain | Residue |
A | ASP432 |
D | ASP455 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD D 542 |
Chain | Residue |
A | HOH550 |
D | ASP94 |
D | GLU96 |
D | HOH571 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD D 543 |
Chain | Residue |
C | GLU16 |
C | CD542 |
D | ARG19 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT D 544 |
Chain | Residue |
A | ARG459 |
A | CD543 |
A | HOH635 |
D | ARG459 |
D | CD539 |
site_id | DC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD E 539 |
Chain | Residue |
E | ASP432 |
E | ACT544 |
E | ACT545 |
E | HOH791 |
G | HIS456 |
G | HOH809 |
site_id | DC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD E 540 |
Chain | Residue |
E | GLU352 |
E | HOH794 |
F | GLU16 |
F | HOH795 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD E 541 |
Chain | Residue |
E | GLU343 |
E | HOH555 |
F | GLU343 |
F | HOH583 |
site_id | DC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD E 542 |
Chain | Residue |
E | GLU224 |
E | HOH819 |
E | HOH820 |
E | HOH821 |
site_id | EC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD E 543 |
Chain | Residue |
E | GLU436 |
G | ASP455 |
site_id | EC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT E 544 |
Chain | Residue |
E | ASP432 |
E | HIS456 |
E | CD539 |
E | HOH791 |
G | GLU298 |
G | ASN453 |
G | HIS456 |
G | HOH808 |
site_id | EC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT E 545 |
Chain | Residue |
E | ASP432 |
E | CD539 |
G | ASP455 |
G | HIS456 |
G | ARG459 |
G | HOH807 |
G | HOH809 |
site_id | EC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD F 539 |
Chain | Residue |
F | ACT543 |
F | ACT544 |
F | HOH824 |
H | CD539 |
H | ACT542 |
site_id | EC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD F 540 |
Chain | Residue |
F | GLU224 |
H | LYS108 |
site_id | EC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD F 541 |
Chain | Residue |
F | ASP393 |
site_id | EC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD F 542 |
Chain | Residue |
F | ASP455 |
site_id | EC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT F 543 |
Chain | Residue |
F | GLU298 |
F | HIS456 |
F | CD539 |
F | HOH824 |
H | HIS456 |
H | CD539 |
site_id | EC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT F 544 |
Chain | Residue |
F | ASP432 |
F | ARG459 |
F | CD539 |
F | HOH824 |
H | ASP455 |
H | ACT542 |
site_id | FC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD G 539 |
Chain | Residue |
G | GLU433 |
site_id | FC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD G 540 |
Chain | Residue |
E | ASP299 |
E | HIS456 |
E | HOH550 |
G | GLU298 |
G | HOH806 |
site_id | FC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD G 541 |
Chain | Residue |
G | ASP432 |
G | HOH807 |
G | HOH808 |
G | HOH809 |
site_id | FC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD G 542 |
Chain | Residue |
G | GLU16 |
G | CD543 |
H | HOH823 |
site_id | FC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD G 543 |
Chain | Residue |
G | GLU23 |
G | CD542 |
G | HOH822 |
H | GLU16 |
H | HOH823 |
site_id | FC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD G 544 |
Chain | Residue |
G | ASP94 |
G | GLU96 |
site_id | FC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD H 539 |
Chain | Residue |
F | HIS456 |
F | CD539 |
F | ACT543 |
H | ASP432 |
H | ACT542 |
site_id | FC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD H 540 |
Chain | Residue |
H | GLU224 |
H | HOH597 |
site_id | FC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD H 541 |
Chain | Residue |
H | ASP94 |
H | GLU96 |
H | HOH547 |
site_id | GC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT H 542 |
Chain | Residue |
F | HIS456 |
F | ARG459 |
F | CD539 |
F | ACT544 |
H | ARG459 |
H | CD539 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgFAGQKCSAGS |
Chain | Residue | Details |
A | PHE314-SER325 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. AEMGGKDT |
Chain | Residue | Details |
A | ALA286-THR293 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00733 |
Chain | Residue | Details |
A | GLU287 | |
E | CYS321 | |
F | GLU287 | |
F | CYS321 | |
G | GLU287 | |
G | CYS321 | |
H | GLU287 | |
H | CYS321 | |
A | CYS321 | |
B | GLU287 | |
B | CYS321 | |
C | GLU287 | |
C | CYS321 | |
D | GLU287 | |
D | CYS321 | |
E | GLU287 |