4MWA
1.85 Angstrom Crystal Structure of GCPE Protein from Bacillus anthracis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016114 | biological_process | terpenoid biosynthetic process |
A | 0044237 | biological_process | cellular metabolic process |
A | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
B | 0016114 | biological_process | terpenoid biosynthetic process |
B | 0044237 | biological_process | cellular metabolic process |
B | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
C | 0016114 | biological_process | terpenoid biosynthetic process |
C | 0044237 | biological_process | cellular metabolic process |
C | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
D | 0016114 | biological_process | terpenoid biosynthetic process |
D | 0044237 | biological_process | cellular metabolic process |
D | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
E | 0016114 | biological_process | terpenoid biosynthetic process |
E | 0044237 | biological_process | cellular metabolic process |
E | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
F | 0016114 | biological_process | terpenoid biosynthetic process |
F | 0044237 | biological_process | cellular metabolic process |
F | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
G | 0016114 | biological_process | terpenoid biosynthetic process |
G | 0044237 | biological_process | cellular metabolic process |
G | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
H | 0016114 | biological_process | terpenoid biosynthetic process |
H | 0044237 | biological_process | cellular metabolic process |
H | 0046429 | molecular_function | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin) |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ARG58 |
A | ARG131 |
A | LYS179 |
A | HIS202 |
A | GLY204 |
A | ARG235 |
A | HOH509 |
A | HOH510 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 402 |
Chain | Residue |
A | ARG90 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 401 |
Chain | Residue |
B | GLN29 |
B | ARG58 |
B | LYS179 |
B | HIS202 |
B | ARG235 |
B | HOH622 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 402 |
Chain | Residue |
B | SER208 |
B | GLY209 |
G | LYS47 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 403 |
Chain | Residue |
B | ARG90 |
B | ARG90 |
B | ARG90 |
B | LYS94 |
B | LYS94 |
B | LYS94 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 401 |
Chain | Residue |
C | ARG58 |
C | ARG131 |
C | LYS179 |
C | HIS202 |
C | ARG235 |
C | SER237 |
C | HOH558 |
C | HOH608 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 402 |
Chain | Residue |
C | SER208 |
C | GLY209 |
C | HOH509 |
C | HOH551 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 403 |
Chain | Residue |
C | ARG112 |
C | LYS115 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 404 |
Chain | Residue |
C | GLU167 |
C | HIS172 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 405 |
Chain | Residue |
C | TYR89 |
C | ARG90 |
C | ARG112 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 401 |
Chain | Residue |
D | SER208 |
D | GLY209 |
D | HOH613 |
E | LYS47 |
E | GLN76 |
E | ASN78 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 402 |
Chain | Residue |
D | LYS115 |
D | LYS115 |
D | LYS115 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 401 |
Chain | Residue |
E | ARG58 |
E | ARG131 |
E | LYS179 |
E | HIS202 |
E | ARG235 |
E | HOH529 |
E | HOH534 |
E | HOH625 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 402 |
Chain | Residue |
E | GLY111 |
E | ARG112 |
E | LYS115 |
F | LYS75 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 401 |
Chain | Residue |
F | ARG58 |
F | ARG131 |
F | LYS179 |
F | HIS202 |
F | ARG235 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 402 |
Chain | Residue |
F | ARG112 |
F | ARG113 |
F | HIS114 |
G | HOH610 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL F 403 |
Chain | Residue |
F | SER208 |
F | GLY209 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 404 |
Chain | Residue |
F | LYS115 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 G 401 |
Chain | Residue |
G | ARG58 |
G | ARG131 |
G | LYS179 |
G | HIS202 |
G | GLY204 |
G | ARG235 |
G | HOH526 |
G | HOH562 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 402 |
Chain | Residue |
G | GLY111 |
G | ARG112 |
G | LYS115 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 H 401 |
Chain | Residue |
H | GLN29 |
H | ARG58 |
H | ARG104 |
H | ARG131 |
H | LYS179 |
H | HIS202 |
H | ARG235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00159 |
Chain | Residue | Details |
E | CYS268 | |
E | CYS271 | |
F | CYS268 | |
F | CYS271 | |
H | CYS268 | |
H | CYS271 |