4QNK
The structure of wt A. thaliana IGPD2 in complex with Mn2+ and phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000105 | biological_process | L-histidine biosynthetic process |
A | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
B | 0000105 | biological_process | L-histidine biosynthetic process |
B | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
C | 0000105 | biological_process | L-histidine biosynthetic process |
C | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
D | 0000105 | biological_process | L-histidine biosynthetic process |
D | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
E | 0000105 | biological_process | L-histidine biosynthetic process |
E | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
F | 0000105 | biological_process | L-histidine biosynthetic process |
F | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
G | 0000105 | biological_process | L-histidine biosynthetic process |
G | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
H | 0000105 | biological_process | L-histidine biosynthetic process |
H | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 301 |
Chain | Residue |
A | HIS47 |
A | HIS169 |
A | GLU173 |
A | HOH417 |
D | HIS74 |
D | HOH478 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 302 |
Chain | Residue |
A | HOH424 |
B | HIS170 |
B | HOH410 |
A | HIS73 |
A | GLU77 |
A | HIS145 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 303 |
Chain | Residue |
A | GLN51 |
A | HIS55 |
A | LYS177 |
A | HOH551 |
H | ARG99 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 304 |
Chain | Residue |
A | GLY96 |
A | SER189 |
A | ASP190 |
A | ARG193 |
A | HOH479 |
A | HOH548 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 301 |
Chain | Residue |
A | HIS74 |
B | HIS47 |
B | HIS169 |
B | GLU173 |
B | HOH412 |
B | HOH548 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 302 |
Chain | Residue |
B | HIS73 |
B | GLU77 |
B | HIS145 |
B | HOH441 |
C | HIS170 |
C | HOH405 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 303 |
Chain | Residue |
B | GLN51 |
B | HIS55 |
B | ARG99 |
B | LYS177 |
B | HOH559 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | ASN98 |
B | GLU188 |
B | SER189 |
B | HOH543 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 305 |
Chain | Residue |
B | GLY96 |
B | SER189 |
B | ASP190 |
B | ARG193 |
B | HOH487 |
B | HOH556 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 301 |
Chain | Residue |
B | HIS74 |
C | HIS47 |
C | HIS169 |
C | GLU173 |
C | HOH536 |
C | HOH539 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 302 |
Chain | Residue |
C | HIS73 |
C | GLU77 |
C | HIS145 |
C | HOH547 |
D | HIS170 |
D | HOH514 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 303 |
Chain | Residue |
A | ARG99 |
C | GLN51 |
C | HIS55 |
C | LYS177 |
C | HOH512 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 304 |
Chain | Residue |
C | LEU88 |
C | ARG94 |
C | LEU118 |
C | SER119 |
C | GLY120 |
C | SER154 |
C | GLY155 |
C | HOH563 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 305 |
Chain | Residue |
C | GLY96 |
C | SER189 |
C | ASP190 |
C | ARG193 |
C | HOH462 |
C | HOH498 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 301 |
Chain | Residue |
A | HIS170 |
A | HOH408 |
D | HIS73 |
D | GLU77 |
D | HIS145 |
D | HOH417 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 302 |
Chain | Residue |
C | HIS74 |
D | HIS47 |
D | HIS169 |
D | GLU173 |
D | HOH428 |
D | HOH471 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 D 303 |
Chain | Residue |
D | GLN51 |
D | HIS55 |
D | LYS177 |
G | ARG99 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 304 |
Chain | Residue |
D | ASP190 |
D | ARG193 |
D | HOH520 |
D | HOH532 |
D | GLY96 |
D | SER189 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 301 |
Chain | Residue |
E | HIS47 |
E | HIS169 |
E | GLU173 |
E | HOH404 |
H | HIS74 |
H | HOH535 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 302 |
Chain | Residue |
E | HIS73 |
E | GLU77 |
E | HIS145 |
E | HOH456 |
F | HIS170 |
F | HOH408 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 E 303 |
Chain | Residue |
D | ARG99 |
E | GLN51 |
E | HIS55 |
E | LYS177 |
E | HOH560 |
E | HOH561 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 304 |
Chain | Residue |
E | LEU88 |
E | LEU118 |
E | SER119 |
E | GLY120 |
E | SER154 |
E | GLY155 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA E 305 |
Chain | Residue |
E | GLY96 |
E | SER189 |
E | ASP190 |
E | ARG193 |
E | HOH405 |
E | HOH500 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 301 |
Chain | Residue |
E | HIS74 |
F | HIS47 |
F | HIS169 |
F | GLU173 |
F | HOH429 |
F | HOH469 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 302 |
Chain | Residue |
F | HIS73 |
F | GLU77 |
F | HIS145 |
F | HOH428 |
G | HIS170 |
G | HOH405 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 F 303 |
Chain | Residue |
F | GLN51 |
F | HIS55 |
F | ARG99 |
F | LYS177 |
F | HOH509 |
F | HOH548 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA F 304 |
Chain | Residue |
F | GLY96 |
F | SER189 |
F | ASP190 |
F | ARG193 |
F | HOH540 |
F | HOH546 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN G 301 |
Chain | Residue |
F | HIS74 |
G | HIS47 |
G | HIS169 |
G | GLU173 |
G | HOH404 |
G | HOH539 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN G 302 |
Chain | Residue |
G | HIS73 |
G | GLU77 |
G | HIS145 |
G | HOH424 |
H | HIS170 |
H | HOH418 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 G 303 |
Chain | Residue |
E | ARG99 |
G | GLN51 |
G | HIS55 |
G | LYS177 |
G | HOH506 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO G 304 |
Chain | Residue |
G | LEU88 |
G | LEU118 |
G | SER119 |
G | GLY120 |
G | SER154 |
G | GLY155 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA G 305 |
Chain | Residue |
G | GLY96 |
G | SER189 |
G | ASP190 |
G | ARG193 |
G | HOH525 |
G | HOH538 |
site_id | DC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN H 301 |
Chain | Residue |
E | HIS170 |
E | HOH422 |
H | HIS73 |
H | GLU77 |
H | HIS145 |
H | HOH429 |
site_id | DC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN H 302 |
Chain | Residue |
G | HIS74 |
H | HIS47 |
H | HIS169 |
H | GLU173 |
H | HOH420 |
H | HOH491 |
site_id | DC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 H 303 |
Chain | Residue |
C | ARG99 |
H | GLN51 |
H | HIS55 |
H | LYS177 |
H | HOH507 |
site_id | DC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA H 304 |
Chain | Residue |
H | GLY96 |
H | SER189 |
H | ASP190 |
H | ARG193 |
H | HOH504 |
H | HOH531 |
Functional Information from PROSITE/UniProt
site_id | PS00954 |
Number of Residues | 14 |
Details | IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IDdHHtnEdvALAI |
Chain | Residue | Details |
A | ILE70-ILE83 |
site_id | PS00955 |
Number of Residues | 13 |
Details | IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GkNsHHiiEAtFK |
Chain | Residue | Details |
A | GLY165-LYS177 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27717128, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
Chain | Residue | Details |
A | GLU21 | |
B | GLU21 | |
C | GLU21 | |
D | GLU21 | |
E | GLU21 | |
F | GLU21 | |
G | GLU21 | |
H | GLU21 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
Chain | Residue | Details |
A | HIS47 | |
C | HIS74 | |
C | HIS169 | |
C | GLU173 | |
D | HIS47 | |
D | HIS74 | |
D | HIS169 | |
D | GLU173 | |
E | HIS47 | |
E | HIS74 | |
E | HIS169 | |
A | HIS74 | |
E | GLU173 | |
F | HIS47 | |
F | HIS74 | |
F | HIS169 | |
F | GLU173 | |
G | HIS47 | |
G | HIS74 | |
G | HIS169 | |
G | GLU173 | |
H | HIS47 | |
A | HIS169 | |
H | HIS74 | |
H | HIS169 | |
H | GLU173 | |
A | GLU173 | |
B | HIS47 | |
B | HIS74 | |
B | HIS169 | |
B | GLU173 | |
C | HIS47 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5ELW |
Chain | Residue | Details |
A | HIS73 | |
C | GLU77 | |
C | HIS145 | |
C | HIS170 | |
D | HIS73 | |
D | GLU77 | |
D | HIS145 | |
D | HIS170 | |
E | HIS73 | |
E | GLU77 | |
E | HIS145 | |
A | GLU77 | |
E | HIS170 | |
F | HIS73 | |
F | GLU77 | |
F | HIS145 | |
F | HIS170 | |
G | HIS73 | |
G | GLU77 | |
G | HIS145 | |
G | HIS170 | |
H | HIS73 | |
A | HIS145 | |
H | GLU77 | |
H | HIS145 | |
H | HIS170 | |
A | HIS170 | |
B | HIS73 | |
B | GLU77 | |
B | HIS145 | |
B | HIS170 | |
C | HIS73 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
Chain | Residue | Details |
A | ARG99 | |
B | ARG99 | |
C | ARG99 | |
D | ARG99 | |
E | ARG99 | |
F | ARG99 | |
G | ARG99 | |
H | ARG99 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
Chain | Residue | Details |
A | ARG121 | |
E | SER199 | |
F | ARG121 | |
F | SER199 | |
G | ARG121 | |
G | SER199 | |
H | ARG121 | |
H | SER199 | |
A | SER199 | |
B | ARG121 | |
B | SER199 | |
C | ARG121 | |
C | SER199 | |
D | ARG121 | |
D | SER199 | |
E | ARG121 |