2ARK
Structure of a flavodoxin from Aquifex aeolicus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0010181 | molecular_function | FMN binding |
A | 0016020 | cellular_component | membrane |
B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0010181 | molecular_function | FMN binding |
B | 0016020 | cellular_component | membrane |
C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
C | 0009055 | molecular_function | electron transfer activity |
C | 0010181 | molecular_function | FMN binding |
C | 0016020 | cellular_component | membrane |
D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
D | 0009055 | molecular_function | electron transfer activity |
D | 0010181 | molecular_function | FMN binding |
D | 0016020 | cellular_component | membrane |
E | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
E | 0009055 | molecular_function | electron transfer activity |
E | 0010181 | molecular_function | FMN binding |
E | 0016020 | cellular_component | membrane |
F | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
F | 0009055 | molecular_function | electron transfer activity |
F | 0010181 | molecular_function | FMN binding |
F | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | THR10 |
A | ARG11 |
A | THR12 |
A | GLY13 |
A | ASN14 |
A | THR15 |
A | PRO58 |
A | HOH513 |
A | HOH576 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 502 |
Chain | Residue |
B | THR10 |
B | ARG11 |
B | THR12 |
B | GLY13 |
B | ASN14 |
B | THR15 |
B | PRO58 |
B | HOH541 |
B | HOH564 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 C 503 |
Chain | Residue |
C | THR10 |
C | ARG11 |
C | THR12 |
C | GLY13 |
C | ASN14 |
C | THR15 |
C | PRO58 |
C | HOH522 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 D 504 |
Chain | Residue |
D | THR10 |
D | ARG11 |
D | THR12 |
D | GLY13 |
D | ASN14 |
D | THR15 |
D | PRO58 |
D | HOH522 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 E 505 |
Chain | Residue |
E | THR10 |
E | ARG11 |
E | THR12 |
E | GLY13 |
E | ASN14 |
E | THR15 |
E | PRO58 |
E | HOH521 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 F 506 |
Chain | Residue |
F | THR10 |
F | ARG11 |
F | THR12 |
F | GLY13 |
F | ASN14 |
F | THR15 |
F | PRO58 |
F | HOH519 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 507 |
Chain | Residue |
A | GOL512 |
B | SER107 |
B | THR110 |
D | VAL103 |
D | MSE106 |
D | SER107 |
D | THR110 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 508 |
Chain | Residue |
A | THR110 |
A | GOL512 |
C | VAL103 |
C | MSE106 |
C | SER107 |
C | THR110 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 509 |
Chain | Residue |
A | ARG156 |
A | ARG157 |
A | GLU160 |
A | ASP179 |
A | HOH522 |
A | HOH524 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 510 |
Chain | Residue |
A | ASP40 |
A | HOH557 |
B | HOH538 |
C | GOL511 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 511 |
Chain | Residue |
B | GOL510 |
C | TYR125 |
C | HOH533 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 512 |
Chain | Residue |
A | MSE106 |
C | GOL508 |
D | GOL507 |
Functional Information from PROSITE/UniProt
site_id | PS00201 |
Number of Residues | 17 |
Details | FLAVODOXIN Flavodoxin signature. VIYdTRtGnTKkmAElV |
Chain | Residue | Details |
A | VAL6-VAL22 |