5Z2L
Crystal structure of BdcA in complex with NADPH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0035438 | molecular_function | cyclic-di-GMP binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0044010 | biological_process | single-species biofilm formation |
A | 0070402 | molecular_function | NADPH binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0035438 | molecular_function | cyclic-di-GMP binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0044010 | biological_process | single-species biofilm formation |
B | 0070402 | molecular_function | NADPH binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0035438 | molecular_function | cyclic-di-GMP binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0044010 | biological_process | single-species biofilm formation |
C | 0070402 | molecular_function | NADPH binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0035438 | molecular_function | cyclic-di-GMP binding |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0044010 | biological_process | single-species biofilm formation |
D | 0070402 | molecular_function | NADPH binding |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0035438 | molecular_function | cyclic-di-GMP binding |
E | 0042803 | molecular_function | protein homodimerization activity |
E | 0044010 | biological_process | single-species biofilm formation |
E | 0070402 | molecular_function | NADPH binding |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0035438 | molecular_function | cyclic-di-GMP binding |
F | 0042803 | molecular_function | protein homodimerization activity |
F | 0044010 | biological_process | single-species biofilm formation |
F | 0070402 | molecular_function | NADPH binding |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0035438 | molecular_function | cyclic-di-GMP binding |
G | 0042803 | molecular_function | protein homodimerization activity |
G | 0044010 | biological_process | single-species biofilm formation |
G | 0070402 | molecular_function | NADPH binding |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0035438 | molecular_function | cyclic-di-GMP binding |
H | 0042803 | molecular_function | protein homodimerization activity |
H | 0044010 | biological_process | single-species biofilm formation |
H | 0070402 | molecular_function | NADPH binding |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0035438 | molecular_function | cyclic-di-GMP binding |
I | 0042803 | molecular_function | protein homodimerization activity |
I | 0044010 | biological_process | single-species biofilm formation |
I | 0070402 | molecular_function | NADPH binding |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0035438 | molecular_function | cyclic-di-GMP binding |
J | 0042803 | molecular_function | protein homodimerization activity |
J | 0044010 | biological_process | single-species biofilm formation |
J | 0070402 | molecular_function | NADPH binding |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0035438 | molecular_function | cyclic-di-GMP binding |
K | 0042803 | molecular_function | protein homodimerization activity |
K | 0044010 | biological_process | single-species biofilm formation |
K | 0070402 | molecular_function | NADPH binding |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0035438 | molecular_function | cyclic-di-GMP binding |
L | 0042803 | molecular_function | protein homodimerization activity |
L | 0044010 | biological_process | single-species biofilm formation |
L | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue PG0 A 301 |
Chain | Residue |
A | GLY89 |
A | ALA141 |
C | HIS240 |
C | HIS242 |
site_id | AC2 |
Number of Residues | 33 |
Details | binding site for residue NDP A 302 |
Chain | Residue |
A | ALA38 |
A | GLY39 |
A | SER40 |
A | THR58 |
A | ASP59 |
A | SER60 |
A | ASN82 |
A | ALA83 |
A | GLY84 |
A | ILE85 |
A | ILE105 |
A | ILE130 |
A | GLY131 |
A | SER132 |
A | TYR146 |
A | LYS150 |
A | PRO176 |
A | GLY177 |
A | PRO178 |
A | ILE179 |
A | THR181 |
A | ALA183 |
A | ASN184 |
A | HOH406 |
A | HOH421 |
A | HOH446 |
A | HOH454 |
A | HOH473 |
A | SER15 |
A | ARG16 |
A | GLY17 |
A | ILE18 |
A | TYR37 |
site_id | AC3 |
Number of Residues | 35 |
Details | binding site for residue NDP D 301 |
Chain | Residue |
D | SER15 |
D | ARG16 |
D | GLY17 |
D | ILE18 |
D | TYR37 |
D | ALA38 |
D | GLY39 |
D | SER40 |
D | THR58 |
D | ASP59 |
D | SER60 |
D | ASN82 |
D | ALA83 |
D | GLY84 |
D | ILE85 |
D | ILE105 |
D | ILE130 |
D | GLY131 |
D | SER132 |
D | TYR146 |
D | LYS150 |
D | PRO176 |
D | GLY177 |
D | PRO178 |
D | ILE179 |
D | THR181 |
D | ALA183 |
D | ASN184 |
D | HOH424 |
D | HOH431 |
D | HOH432 |
D | HOH433 |
D | HOH487 |
D | HOH509 |
D | HOH536 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | VAL140 |
B | MET143 |
B | MET193 |
B | LEU197 |
B | PHE235 |
B | HOH415 |
B | HOH457 |
D | HOH500 |
site_id | AC5 |
Number of Residues | 34 |
Details | binding site for residue NDP B 302 |
Chain | Residue |
B | LYS150 |
B | PRO176 |
B | GLY177 |
B | PRO178 |
B | ILE179 |
B | THR181 |
B | ALA183 |
B | ASN184 |
B | HOH405 |
B | HOH411 |
B | HOH424 |
B | HOH478 |
B | HOH486 |
B | HOH514 |
B | HOH532 |
B | SER15 |
B | ARG16 |
B | GLY17 |
B | ILE18 |
B | TYR37 |
B | ALA38 |
B | GLY39 |
B | SER40 |
B | THR58 |
B | ASP59 |
B | SER60 |
B | ASN82 |
B | ALA83 |
B | GLY84 |
B | ILE105 |
B | ILE130 |
B | GLY131 |
B | SER132 |
B | TYR146 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | VAL133 |
C | ASN134 |
C | PRO176 |
C | GLY177 |
C | ASN184 |
C | PHE235 |
C | NDP304 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | ALA61 |
C | ASP62 |
C | LYS104 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | ASP62 |
C | ARG63 |
C | ASP64 |
C | HOH401 |
C | HOH414 |
site_id | AC9 |
Number of Residues | 35 |
Details | binding site for residue NDP C 304 |
Chain | Residue |
C | SER15 |
C | ARG16 |
C | GLY17 |
C | ILE18 |
C | TYR37 |
C | ALA38 |
C | GLY39 |
C | SER40 |
C | THR58 |
C | ASP59 |
C | SER60 |
C | ASN82 |
C | ALA83 |
C | GLY84 |
C | ILE105 |
C | ILE130 |
C | GLY131 |
C | SER132 |
C | TYR146 |
C | LYS150 |
C | PRO176 |
C | GLY177 |
C | PRO178 |
C | ILE179 |
C | THR181 |
C | ALA183 |
C | ASN184 |
C | GOL301 |
C | HOH428 |
C | HOH431 |
C | HOH433 |
C | HOH451 |
C | HOH483 |
C | HOH494 |
C | HOH561 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL E 301 |
Chain | Residue |
E | TYR146 |
E | ALA183 |
E | NDP303 |
E | HOH418 |
site_id | AD2 |
Number of Residues | 36 |
Details | binding site for residue NDP E 303 |
Chain | Residue |
E | GLY13 |
E | SER15 |
E | ARG16 |
E | GLY17 |
E | ILE18 |
E | TYR37 |
E | ALA38 |
E | GLY39 |
E | SER40 |
E | THR58 |
E | ASP59 |
E | SER60 |
E | ASN82 |
E | ALA83 |
E | GLY84 |
E | ILE85 |
E | ILE105 |
E | ILE130 |
E | GLY131 |
E | SER132 |
E | TYR146 |
E | LYS150 |
E | PRO176 |
E | GLY177 |
E | PRO178 |
E | ILE179 |
E | THR181 |
E | ALA183 |
E | ASN184 |
E | GOL301 |
E | HOH411 |
E | HOH435 |
E | HOH439 |
E | HOH448 |
E | HOH458 |
E | HOH511 |
site_id | AD3 |
Number of Residues | 36 |
Details | binding site for residue NDP J 301 |
Chain | Residue |
J | GLY13 |
J | SER15 |
J | ARG16 |
J | GLY17 |
J | ILE18 |
J | TYR37 |
J | ALA38 |
J | GLY39 |
J | SER40 |
J | THR58 |
J | ASP59 |
J | SER60 |
J | ASN82 |
J | ALA83 |
J | GLY84 |
J | ILE85 |
J | ILE105 |
J | ILE130 |
J | GLY131 |
J | SER132 |
J | TYR146 |
J | LYS150 |
J | PRO176 |
J | GLY177 |
J | PRO178 |
J | ILE179 |
J | THR181 |
J | ALA183 |
J | ASN184 |
J | HOH423 |
J | HOH424 |
J | HOH432 |
J | HOH439 |
J | HOH441 |
J | HOH450 |
J | HOH494 |
site_id | AD4 |
Number of Residues | 31 |
Details | binding site for residue NDP H 301 |
Chain | Residue |
H | SER15 |
H | ARG16 |
H | GLY17 |
H | ILE18 |
H | TYR37 |
H | ALA38 |
H | GLY39 |
H | SER40 |
H | THR58 |
H | ASP59 |
H | SER60 |
H | ASN82 |
H | ALA83 |
H | GLY84 |
H | ILE85 |
H | ILE105 |
H | ILE130 |
H | GLY131 |
H | SER132 |
H | TYR146 |
H | LYS150 |
H | PRO176 |
H | GLY177 |
H | PRO178 |
H | ILE179 |
H | THR181 |
H | ALA183 |
H | ASN184 |
H | HOH403 |
H | HOH404 |
H | HOH454 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue PEG K 301 |
Chain | Residue |
K | ARG202 |
K | GLU207 |
K | GLU208 |
K | HOH496 |
L | ARG24 |
L | GLU50 |
L | HOH420 |
site_id | AD6 |
Number of Residues | 35 |
Details | binding site for residue NDP K 302 |
Chain | Residue |
K | GLY13 |
K | SER15 |
K | ARG16 |
K | GLY17 |
K | ILE18 |
K | TYR37 |
K | ALA38 |
K | GLY39 |
K | SER40 |
K | THR58 |
K | ASP59 |
K | SER60 |
K | ASN82 |
K | ALA83 |
K | GLY84 |
K | ILE105 |
K | ILE130 |
K | GLY131 |
K | SER132 |
K | TYR146 |
K | LYS150 |
K | PRO176 |
K | GLY177 |
K | PRO178 |
K | ILE179 |
K | THR181 |
K | ALA183 |
K | ASN184 |
K | HOH408 |
K | HOH416 |
K | HOH424 |
K | HOH451 |
K | HOH453 |
K | HOH464 |
K | HOH497 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO I 301 |
Chain | Residue |
I | ARG16 |
I | NDP302 |
I | HOH412 |
I | HOH589 |
site_id | AD8 |
Number of Residues | 34 |
Details | binding site for residue NDP I 302 |
Chain | Residue |
I | SER15 |
I | ARG16 |
I | GLY17 |
I | ILE18 |
I | TYR37 |
I | ALA38 |
I | GLY39 |
I | SER40 |
I | THR58 |
I | ASP59 |
I | SER60 |
I | ASN82 |
I | ALA83 |
I | GLY84 |
I | ILE85 |
I | ILE105 |
I | ILE130 |
I | GLY131 |
I | SER132 |
I | TYR146 |
I | LYS150 |
I | PRO176 |
I | GLY177 |
I | PRO178 |
I | ILE179 |
I | THR181 |
I | ALA183 |
I | ASN184 |
I | EDO301 |
I | HOH412 |
I | HOH422 |
I | HOH424 |
I | HOH433 |
I | HOH518 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue PG4 F 301 |
Chain | Residue |
F | HIS240 |
H | GLY89 |
H | ALA141 |
H | GLY142 |
H | MET143 |
site_id | AE1 |
Number of Residues | 37 |
Details | binding site for residue NDP F 302 |
Chain | Residue |
F | GLY13 |
F | SER15 |
F | ARG16 |
F | GLY17 |
F | ILE18 |
F | TYR37 |
F | ALA38 |
F | GLY39 |
F | SER40 |
F | THR58 |
F | ASP59 |
F | SER60 |
F | ASN82 |
F | ALA83 |
F | GLY84 |
F | ILE85 |
F | ARG101 |
F | ILE105 |
F | ILE130 |
F | GLY131 |
F | SER132 |
F | TYR146 |
F | LYS150 |
F | PRO176 |
F | GLY177 |
F | PRO178 |
F | ILE179 |
F | THR181 |
F | ALA183 |
F | ASN184 |
F | HOH410 |
F | HOH419 |
F | HOH437 |
F | HOH447 |
F | HOH485 |
F | HOH487 |
F | HOH494 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue EDO G 301 |
Chain | Residue |
G | HIS240 |
site_id | AE3 |
Number of Residues | 32 |
Details | binding site for residue NDP G 302 |
Chain | Residue |
G | GLY13 |
G | SER15 |
G | ARG16 |
G | GLY17 |
G | ILE18 |
G | TYR37 |
G | ALA38 |
G | GLY39 |
G | SER40 |
G | THR58 |
G | ASP59 |
G | SER60 |
G | ASN82 |
G | ALA83 |
G | GLY84 |
G | ILE105 |
G | ILE130 |
G | GLY131 |
G | SER132 |
G | TYR146 |
G | LYS150 |
G | PRO176 |
G | GLY177 |
G | PRO178 |
G | ILE179 |
G | THR181 |
G | ALA183 |
G | ASN184 |
G | HOH406 |
G | HOH407 |
G | HOH414 |
G | HOH418 |
site_id | AE4 |
Number of Residues | 35 |
Details | binding site for residue NDP L 301 |
Chain | Residue |
L | SER15 |
L | ARG16 |
L | GLY17 |
L | ILE18 |
L | TYR37 |
L | ALA38 |
L | GLY39 |
L | SER40 |
L | THR58 |
L | ASP59 |
L | SER60 |
L | ASN82 |
L | ALA83 |
L | GLY84 |
L | ILE85 |
L | ARG101 |
L | ILE105 |
L | ILE130 |
L | GLY131 |
L | SER132 |
L | TYR146 |
L | LYS150 |
L | PRO176 |
L | GLY177 |
L | PRO178 |
L | ILE179 |
L | THR181 |
L | ALA183 |
L | ASN184 |
L | HOH409 |
L | HOH439 |
L | HOH449 |
L | HOH504 |
L | HOH538 |
L | HOH540 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. VngdrmpvagMaaYAASKSALqGMArGLA |
Chain | Residue | Details |
A | VAL133-ALA161 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR146 | |
F | TYR146 | |
G | TYR146 | |
L | TYR146 | |
D | TYR146 | |
B | TYR146 | |
C | TYR146 | |
E | TYR146 | |
J | TYR146 | |
H | TYR146 | |
K | TYR146 | |
I | TYR146 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LEU10 | |
E | SER132 | |
J | LEU10 | |
J | SER132 | |
H | LEU10 | |
H | SER132 | |
K | LEU10 | |
K | SER132 | |
I | LEU10 | |
I | SER132 | |
F | LEU10 | |
A | SER132 | |
F | SER132 | |
G | LEU10 | |
G | SER132 | |
L | LEU10 | |
L | SER132 | |
D | LEU10 | |
D | SER132 | |
B | LEU10 | |
B | SER132 | |
C | LEU10 | |
C | SER132 | |
E | LEU10 |