5MZ8
Crystal structure of aldehyde dehydrogenase 21 (ALDH21) from Physcomitrella patens in complex with the reaction product succinate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
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 | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
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 | 0000166 | molecular_function | nucleotide binding |
C | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
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 | 0000166 | molecular_function | nucleotide binding |
D | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue SIN A 501 |
Chain | Residue |
A | ARG121 |
A | ASN171 |
A | PHE172 |
A | LEU176 |
A | TYR296 |
A | SER301 |
A | CYS302 |
A | ARG457 |
A | TYR463 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | ASP278 |
A | TYR279 |
A | LYS431 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | LYS263 |
A | VAL264 |
A | HOH650 |
B | LYS263 |
B | VAL264 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | TYR44 |
A | ASN46 |
C | THR45 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LYS158 |
A | LYS477 |
A | ASP481 |
A | HOH606 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | THR41 |
A | ASN46 |
C | ASP47 |
C | VAL48 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | THR103 |
A | MET106 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | PHE159 |
A | GLU485 |
A | LYS487 |
A | HOH649 |
B | LEU466 |
B | HOH619 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | LYS467 |
A | ASP468 |
B | LYS241 |
B | HOH666 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue PEG A 511 |
Chain | Residue |
A | ASP432 |
D | ASP432 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residue PEG A 512 |
Chain | Residue |
A | GLY270 |
A | ASN271 |
A | PRO273 |
A | CYS417 |
A | ASN418 |
A | THR420 |
A | TYR422 |
A | GLY423 |
A | LEU424 |
A | GLN425 |
A | SER426 |
A | VAL445 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue PEG A 513 |
Chain | Residue |
A | LYS150 |
A | ARG492 |
A | ASN493 |
B | TYR285 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue SIN B 501 |
Chain | Residue |
B | ARG121 |
B | ASN171 |
B | PHE172 |
B | LEU176 |
B | TYR296 |
B | SER301 |
B | CYS302 |
B | ARG457 |
B | TYR463 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | GLY332 |
B | LYS374 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | ASP278 |
B | TYR279 |
B | LYS431 |
B | EDO504 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | ARG313 |
B | GLU317 |
B | EDO503 |
B | HOH686 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | LYS477 |
B | ASP481 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
B | ASP481 |
B | LEU484 |
B | GLU485 |
B | THR486 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | GLU92 |
B | ILE209 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue EDO B 508 |
Chain | Residue |
B | GLU92 |
B | ARG96 |
B | LYS212 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue EDO B 509 |
Chain | Residue |
B | ASN23 |
B | PHE25 |
B | GLU208 |
site_id | AE4 |
Number of Residues | 1 |
Details | binding site for residue EDO B 510 |
Chain | Residue |
B | GLN102 |
site_id | AE5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 511 |
Chain | Residue |
B | LYS36 |
B | GLN54 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 512 |
Chain | Residue |
B | LYS194 |
B | VAL226 |
B | SER227 |
B | HOH667 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue EDO B 513 |
Chain | Residue |
B | LEU218 |
site_id | AE8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 514 |
Chain | Residue |
B | ASP282 |
B | HOH701 |
site_id | AE9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 515 |
Chain | Residue |
C | THR369 |
C | GLY370 |
C | ASN372 |
C | GLU379 |
site_id | AF1 |
Number of Residues | 3 |
Details | binding site for residue EDO B 516 |
Chain | Residue |
B | LYS328 |
B | LEU329 |
B | LYS330 |
site_id | AF2 |
Number of Residues | 7 |
Details | binding site for residue PEG B 517 |
Chain | Residue |
B | ILE136 |
B | LYS157 |
B | LYS158 |
B | VAL187 |
B | HOH646 |
B | HOH662 |
C | HIS140 |
site_id | AF3 |
Number of Residues | 3 |
Details | binding site for residue EDO B 518 |
Chain | Residue |
B | ASP432 |
B | ASN434 |
D | LEU497 |
site_id | AF4 |
Number of Residues | 9 |
Details | binding site for residue SIN C 501 |
Chain | Residue |
C | ARG121 |
C | ASN171 |
C | PHE172 |
C | TYR296 |
C | SER301 |
C | CYS302 |
C | ARG457 |
C | TYR463 |
C | HOH623 |
site_id | AF5 |
Number of Residues | 3 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | LYS406 |
C | TYR407 |
C | HOH624 |
site_id | AF6 |
Number of Residues | 5 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | GLU132 |
C | ARG135 |
C | ILE136 |
C | LYS477 |
C | MET480 |
site_id | AF7 |
Number of Residues | 2 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | ASP432 |
C | ASN434 |
site_id | AF8 |
Number of Residues | 3 |
Details | binding site for residue EDO C 505 |
Chain | Residue |
C | ASP278 |
C | TYR279 |
C | LYS431 |
site_id | AF9 |
Number of Residues | 2 |
Details | binding site for residue EDO C 506 |
Chain | Residue |
C | ASP385 |
C | LYS406 |
site_id | AG1 |
Number of Residues | 3 |
Details | binding site for residue EDO C 507 |
Chain | Residue |
C | ASN42 |
C | ASN333 |
C | PHE335 |
site_id | AG2 |
Number of Residues | 2 |
Details | binding site for residue EDO C 508 |
Chain | Residue |
C | GLU99 |
C | LYS212 |
site_id | AG3 |
Number of Residues | 5 |
Details | binding site for residue EDO C 510 |
Chain | Residue |
C | PHE159 |
C | LYS487 |
C | HOH635 |
D | LEU466 |
D | HOH650 |
site_id | AG4 |
Number of Residues | 3 |
Details | binding site for residue EDO C 511 |
Chain | Residue |
C | HIS442 |
C | GLU444 |
C | HOH646 |
site_id | AG5 |
Number of Residues | 4 |
Details | binding site for residue EDO C 512 |
Chain | Residue |
C | VAL236 |
C | ASP237 |
C | GLU238 |
C | ARG239 |
site_id | AG6 |
Number of Residues | 1 |
Details | binding site for residue PEG C 513 |
Chain | Residue |
C | LYS431 |
site_id | AG7 |
Number of Residues | 6 |
Details | binding site for residue PEG C 514 |
Chain | Residue |
C | ASP144 |
C | GLY151 |
C | LEU152 |
C | ASN493 |
C | VAL494 |
C | THR496 |
site_id | AG8 |
Number of Residues | 7 |
Details | binding site for residue EDO D 501 |
Chain | Residue |
A | PRO142 |
A | LEU143 |
A | ILE145 |
B | SER460 |
D | VAL134 |
D | ARG135 |
D | TYR137 |
site_id | AG9 |
Number of Residues | 10 |
Details | binding site for residue SIN D 502 |
Chain | Residue |
D | ARG121 |
D | ASN171 |
D | PHE172 |
D | ASN175 |
D | LEU176 |
D | TYR296 |
D | SER301 |
D | CYS302 |
D | ARG457 |
D | TYR463 |
site_id | AH1 |
Number of Residues | 5 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
D | ALA84 |
D | GLU87 |
D | LYS88 |
D | HOH613 |
D | HOH621 |
site_id | AH2 |
Number of Residues | 6 |
Details | binding site for residue GOL D 504 |
Chain | Residue |
C | LYS263 |
C | VAL264 |
D | LYS256 |
D | LYS263 |
D | VAL264 |
D | ILE471 |
site_id | AH3 |
Number of Residues | 5 |
Details | binding site for residue EDO D 505 |
Chain | Residue |
D | ILE136 |
D | LYS477 |
D | LEU484 |
D | HOH604 |
D | HOH664 |
site_id | AH4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 506 |
Chain | Residue |
D | LYS150 |
D | ARG492 |
D | ASN493 |
site_id | AH5 |
Number of Residues | 3 |
Details | binding site for residue EDO D 507 |
Chain | Residue |
C | ARG473 |
D | GLU485 |
D | THR486 |
site_id | AH6 |
Number of Residues | 2 |
Details | binding site for residue EDO D 508 |
Chain | Residue |
D | ASN42 |
D | PHE335 |
site_id | AH7 |
Number of Residues | 3 |
Details | binding site for residue EDO D 509 |
Chain | Residue |
D | ASN23 |
D | PRO30 |
D | ASP32 |
site_id | AH8 |
Number of Residues | 4 |
Details | binding site for residue EDO D 510 |
Chain | Residue |
D | GLU238 |
D | PHE240 |
D | LYS241 |
D | LYS262 |
site_id | AH9 |
Number of Residues | 4 |
Details | binding site for residue PEG D 511 |
Chain | Residue |
D | GLY151 |
D | VAL494 |
D | THR496 |
D | HOH651 |
Functional Information from PROSITE/UniProt
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGNAP |
Chain | Residue | Details |
A | MET266-PRO273 |