4O8M
Crystal structure of a trap periplasmic solute binding protein actinobacillus succinogenes 130z, target EFI-510004, with bound L-galactonate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0055085 | biological_process | transmembrane transport |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0055085 | biological_process | transmembrane transport |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
C | 0055085 | biological_process | transmembrane transport |
D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
D | 0055085 | biological_process | transmembrane transport |
E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
E | 0055085 | biological_process | transmembrane transport |
F | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
F | 0055085 | biological_process | transmembrane transport |
G | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
G | 0055085 | biological_process | transmembrane transport |
H | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
H | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 401 |
Chain | Residue |
A | THR74 |
A | HIS173 |
A | HOH819 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
C | HOH814 |
A | SER111 |
A | GLN112 |
A | SER113 |
A | LYS116 |
A | HOH829 |
A | HOH880 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2Q2 A 403 |
Chain | Residue |
A | GLU73 |
A | ILE89 |
A | SER90 |
A | ASP91 |
A | TYR147 |
A | ARG150 |
A | ARG170 |
A | GLN172 |
A | LEU193 |
A | ASN210 |
A | HIS235 |
A | SER237 |
A | HOH555 |
A | HOH586 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 401 |
Chain | Residue |
B | THR74 |
B | HIS173 |
B | SER192 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 402 |
Chain | Residue |
B | SER111 |
B | GLN112 |
B | LYS116 |
B | HOH863 |
B | HOH954 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2Q2 B 403 |
Chain | Residue |
B | GLU73 |
B | ILE89 |
B | SER90 |
B | ASP91 |
B | TYR147 |
B | ARG150 |
B | ARG170 |
B | GLN172 |
B | LEU193 |
B | ASN210 |
B | HIS235 |
B | SER237 |
B | HOH528 |
B | HOH604 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 401 |
Chain | Residue |
C | SER72 |
C | GLU73 |
C | THR74 |
C | GLN172 |
C | HIS173 |
C | SER192 |
C | LEU193 |
C | HOH589 |
C | HOH859 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 402 |
Chain | Residue |
C | SER111 |
C | GLN112 |
C | SER113 |
C | LYS116 |
C | HOH646 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2Q2 C 403 |
Chain | Residue |
C | GLU73 |
C | ILE89 |
C | SER90 |
C | ASP91 |
C | TYR147 |
C | ARG150 |
C | ARG170 |
C | GLN172 |
C | LEU193 |
C | ASN210 |
C | HIS235 |
C | SER237 |
C | HOH544 |
C | HOH643 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL D 401 |
Chain | Residue |
D | ASP91 |
D | GLY93 |
D | SER174 |
D | PHE177 |
D | HOH518 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 402 |
Chain | Residue |
A | THR289 |
D | HIS122 |
D | LYS127 |
D | HOH660 |
D | HOH889 |
D | HOH933 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 D 403 |
Chain | Residue |
D | SER72 |
D | GLU73 |
D | THR74 |
D | GLN172 |
D | HIS173 |
D | MET191 |
D | SER192 |
D | LEU193 |
D | HOH546 |
D | HOH576 |
D | HOH650 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 404 |
Chain | Residue |
D | LYS116 |
D | HOH560 |
D | HOH750 |
D | SER111 |
D | GLN112 |
D | SER113 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2Q2 D 405 |
Chain | Residue |
D | GLU73 |
D | ILE89 |
D | SER90 |
D | ASP91 |
D | TYR147 |
D | ARG150 |
D | ARG170 |
D | GLN172 |
D | ASN210 |
D | HIS235 |
D | SER237 |
D | HOH548 |
D | HOH784 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 401 |
Chain | Residue |
E | SER111 |
E | GLN112 |
E | SER113 |
E | LYS116 |
E | HOH883 |
E | HOH951 |
site_id | BC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 2Q2 E 402 |
Chain | Residue |
E | GLU73 |
E | ILE89 |
E | SER90 |
E | ASP91 |
E | TYR147 |
E | ARG150 |
E | ARG170 |
E | GLN172 |
E | LEU193 |
E | ASN210 |
E | HIS235 |
E | SER237 |
E | HOH508 |
E | HOH642 |
E | HOH829 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 F 401 |
Chain | Residue |
F | SER72 |
F | GLU73 |
F | THR74 |
F | HIS173 |
F | SER192 |
F | HOH521 |
F | HOH575 |
F | HOH759 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 402 |
Chain | Residue |
F | SER111 |
F | GLN112 |
F | LYS116 |
F | HOH643 |
site_id | CC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2Q2 F 403 |
Chain | Residue |
F | GLU73 |
F | ILE89 |
F | SER90 |
F | ASP91 |
F | TYR147 |
F | ARG150 |
F | ARG170 |
F | GLN172 |
F | LEU193 |
F | ASN210 |
F | HIS235 |
F | SER237 |
F | HOH529 |
F | HOH622 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 G 401 |
Chain | Residue |
G | HIS136 |
G | HOH713 |
G | HOH723 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 G 402 |
Chain | Residue |
G | SER72 |
G | GLU73 |
G | THR74 |
G | GLN172 |
G | HIS173 |
G | MET191 |
G | SER192 |
G | HOH546 |
G | HOH561 |
G | HOH683 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 G 403 |
Chain | Residue |
G | SER111 |
G | GLN112 |
G | SER113 |
G | LYS116 |
G | HOH577 |
G | HOH799 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 G 404 |
Chain | Residue |
G | HIS122 |
G | ARG262 |
G | HOH649 |
G | HOH724 |
G | HOH821 |
G | HOH932 |
site_id | CC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2Q2 G 405 |
Chain | Residue |
G | GLU73 |
G | ILE89 |
G | SER90 |
G | ASP91 |
G | TYR147 |
G | ARG150 |
G | ARG170 |
G | GLN172 |
G | ASN210 |
G | HIS235 |
G | SER237 |
G | HOH559 |
G | HOH702 |
site_id | CC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 H 401 |
Chain | Residue |
H | SER72 |
H | GLU73 |
H | THR74 |
H | ARG170 |
H | GLN172 |
H | HIS173 |
H | SER192 |
H | LEU193 |
H | HOH585 |
H | HOH587 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 H 402 |
Chain | Residue |
H | SER111 |
H | GLN112 |
H | SER113 |
H | LYS116 |
H | HOH625 |
H | HOH697 |
H | HOH790 |
H | HOH857 |
site_id | CC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2Q2 H 403 |
Chain | Residue |
H | GLU73 |
H | ILE89 |
H | SER90 |
H | ASP91 |
H | TYR147 |
H | ARG150 |
H | ARG170 |
H | GLN172 |
H | LEU193 |
H | ASN210 |
H | HIS235 |
H | SER237 |
H | HOH520 |
H | HOH933 |
Functional Information from PROSITE/UniProt
site_id | PS00160 |
Number of Residues | 14 |
Details | ALDOLASE_KDPG_KHG_2 KDPG and KHG aldolases Schiff-base forming residue. GdivFKLFPSsqlG |
Chain | Residue | Details |
A | GLY58-GLY71 |