6YAV
Structure of FeSII (Shethna) protein from Azotobacter vinelandii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0046872 | molecular_function | metal ion binding |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0046872 | molecular_function | metal ion binding |
E | 0051536 | molecular_function | iron-sulfur cluster binding |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue FES E 201 |
Chain | Residue |
E | GLU41 |
E | CYS42 |
E | GLY45 |
E | CYS47 |
E | GLY48 |
E | CYS50 |
E | CYS102 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL E 202 |
Chain | Residue |
E | ARG99 |
E | GLU109 |
E | HOH302 |
E | HOH331 |
E | ARG61 |
E | LEU66 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG E 203 |
Chain | Residue |
E | SER8 |
E | MET11 |
E | HOH322 |
E | HOH343 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue FES A 5000 |
Chain | Residue |
A | PHE40 |
A | GLU41 |
A | CYS42 |
A | GLY45 |
A | CYS47 |
A | GLY48 |
A | SER49 |
A | CYS50 |
A | CYS102 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue FES B 5000 |
Chain | Residue |
B | PHE40 |
B | GLU41 |
B | CYS42 |
B | GLY45 |
B | CYS47 |
B | GLY48 |
B | SER49 |
B | CYS50 |
B | CYS102 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue FES C 5000 |
Chain | Residue |
C | GLU41 |
C | CYS42 |
C | GLY45 |
C | CYS47 |
C | GLY48 |
C | SER49 |
C | CYS50 |
C | CYS102 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue FES D 201 |
Chain | Residue |
D | PHE40 |
D | GLU41 |
D | CYS42 |
D | GLY45 |
D | CYS47 |
D | GLY48 |
D | CYS50 |
D | CYS102 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL D 202 |
Chain | Residue |
C | LYS53 |
C | THR55 |
C | GLU114 |
D | LYS53 |
D | THR55 |
D | GLU114 |
Functional Information from PROSITE/UniProt
site_id | PS00197 |
Number of Residues | 9 |
Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CQDGNCGSC |
Chain | Residue | Details |
E | CYS42-CYS50 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:26654855 |
Chain | Residue | Details |
E | CYS42 | |
B | CYS47 | |
B | CYS50 | |
B | CYS102 | |
C | CYS42 | |
C | CYS47 | |
C | CYS50 | |
C | CYS102 | |
D | CYS42 | |
D | CYS47 | |
D | CYS50 | |
E | CYS47 | |
D | CYS102 | |
E | CYS50 | |
E | CYS102 | |
A | CYS42 | |
A | CYS47 | |
A | CYS50 | |
A | CYS102 | |
B | CYS42 |