5OVW
Nanobody-bound BtuF, the vitamin B12 binding protein in Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0015889 | biological_process | cobalamin transport |
A | 0031419 | molecular_function | cobalamin binding |
A | 0042597 | cellular_component | periplasmic space |
B | 0015889 | biological_process | cobalamin transport |
B | 0031419 | molecular_function | cobalamin binding |
B | 0042597 | cellular_component | periplasmic space |
C | 0015889 | biological_process | cobalamin transport |
C | 0031419 | molecular_function | cobalamin binding |
C | 0042597 | cellular_component | periplasmic space |
D | 0015889 | biological_process | cobalamin transport |
D | 0031419 | molecular_function | cobalamin binding |
D | 0042597 | cellular_component | periplasmic space |
E | 0015889 | biological_process | cobalamin transport |
E | 0031419 | molecular_function | cobalamin binding |
E | 0042597 | cellular_component | periplasmic space |
F | 0015889 | biological_process | cobalamin transport |
F | 0031419 | molecular_function | cobalamin binding |
F | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | PHE168 |
B | TRP196 |
B | GLN198 |
I | TYR54 |
I | PHE125 |
I | TYR136 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL D 301 |
Chain | Residue |
D | HOH401 |
J | TYR54 |
J | TYR136 |
D | PHE168 |
D | TRP196 |
D | GLN198 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL E 301 |
Chain | Residue |
E | PHE168 |
E | TRP196 |
E | GLN198 |
K | TYR54 |
K | PHE125 |
K | TYR136 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL F 301 |
Chain | Residue |
F | PHE168 |
F | TRP196 |
F | GLN198 |
L | TYR54 |
L | TYR136 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL H 201 |
Chain | Residue |
A | TRP196 |
A | GLN198 |
H | TYR54 |
H | TYR136 |
H | HOH306 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01000, ECO:0000269|PubMed:12468528, ECO:0007744|PDB:1N4A |
Chain | Residue | Details |
A | TYR50 | |
B | TYR50 | |
C | TYR50 | |
D | TYR50 | |
E | TYR50 | |
F | TYR50 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01000, ECO:0000269|PubMed:12468528, ECO:0000269|PubMed:12475936, ECO:0007744|PDB:1N2Z, ECO:0007744|PDB:1N4A |
Chain | Residue | Details |
A | ASP242 | |
B | ASP242 | |
C | ASP242 | |
D | ASP242 | |
E | ASP242 | |
F | ASP242 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | SITE: Important for BtuC binding => ECO:0000255|HAMAP-Rule:MF_01000, ECO:0000305|PubMed:12475936 |
Chain | Residue | Details |
A | GLU72 | |
E | GLU202 | |
F | GLU72 | |
F | GLU202 | |
A | GLU202 | |
B | GLU72 | |
B | GLU202 | |
C | GLU72 | |
C | GLU202 | |
D | GLU72 | |
D | GLU202 | |
E | GLU72 |