3TG0
E. coli alkaline phosphatase with bound inorganic phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004035 | molecular_function | alkaline phosphatase activity |
A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
A | 0033748 | molecular_function | hydrogenase (acceptor) activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004035 | molecular_function | alkaline phosphatase activity |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
B | 0033748 | molecular_function | hydrogenase (acceptor) activity |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004035 | molecular_function | alkaline phosphatase activity |
C | 0004721 | molecular_function | phosphoprotein phosphatase activity |
C | 0005515 | molecular_function | protein binding |
C | 0006470 | biological_process | protein dephosphorylation |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016791 | molecular_function | phosphatase activity |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
C | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
C | 0033748 | molecular_function | hydrogenase (acceptor) activity |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004035 | molecular_function | alkaline phosphatase activity |
D | 0004721 | molecular_function | phosphoprotein phosphatase activity |
D | 0005515 | molecular_function | protein binding |
D | 0006470 | biological_process | protein dephosphorylation |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016791 | molecular_function | phosphatase activity |
D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
D | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
D | 0033748 | molecular_function | hydrogenase (acceptor) activity |
D | 0042597 | cellular_component | periplasmic space |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | ASP51 |
A | SER102 |
A | ASP327 |
A | ASP369 |
A | HIS370 |
A | PO4504 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | PO4504 |
A | ASP327 |
A | HIS331 |
A | HIS412 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | ASP51 |
A | THR155 |
A | GLU322 |
A | HOH5060 |
A | HOH5124 |
A | HOH5275 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PO4 A 504 |
Chain | Residue |
A | ASP51 |
A | SER102 |
A | ARG166 |
A | ASP327 |
A | HIS331 |
A | HIS370 |
A | HIS412 |
A | ZN501 |
A | ZN502 |
A | HOH5189 |
A | HOH5275 |
A | HOH6264 |
A | HOH6450 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 505 |
Chain | Residue |
B | ASP327 |
B | HIS331 |
B | HIS412 |
B | PO4508 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 506 |
Chain | Residue |
B | ASP51 |
B | SER102 |
B | ASP369 |
B | HIS370 |
B | PO4508 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 507 |
Chain | Residue |
B | ASP51 |
B | THR155 |
B | GLU322 |
B | HOH5001 |
B | HOH5093 |
B | HOH5117 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PO4 B 508 |
Chain | Residue |
B | ASP51 |
B | ASP101 |
B | SER102 |
B | ARG166 |
B | ASP327 |
B | HIS331 |
B | HIS370 |
B | HIS412 |
B | ZN505 |
B | ZN506 |
B | HOH5054 |
B | HOH5117 |
B | HOH6160 |
B | HOH6503 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 509 |
Chain | Residue |
C | ASP51 |
C | SER102 |
C | ASP327 |
C | ASP369 |
C | HIS370 |
C | PO4512 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 510 |
Chain | Residue |
C | ASP327 |
C | HIS331 |
C | HIS412 |
C | PO4512 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 511 |
Chain | Residue |
C | ASP51 |
C | THR155 |
C | GLU322 |
C | HOH5002 |
C | HOH5232 |
C | HOH6210 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PO4 C 512 |
Chain | Residue |
C | ASP51 |
C | SER102 |
C | ARG166 |
C | ASP327 |
C | HIS331 |
C | HIS370 |
C | HIS412 |
C | ZN509 |
C | ZN510 |
C | HOH5330 |
C | HOH6210 |
C | HOH6497 |
C | HOH6614 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 513 |
Chain | Residue |
D | ASP51 |
D | SER102 |
D | ASP369 |
D | HIS370 |
D | PO4516 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 514 |
Chain | Residue |
D | ASP327 |
D | HIS331 |
D | HIS412 |
D | PO4516 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 515 |
Chain | Residue |
D | HOH5098 |
D | HOH5112 |
D | HOH5158 |
D | ASP51 |
D | THR155 |
D | GLU322 |
site_id | BC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PO4 D 516 |
Chain | Residue |
D | ASP51 |
D | ASP101 |
D | SER102 |
D | ARG166 |
D | ASP327 |
D | HIS331 |
D | HIS370 |
D | HIS412 |
D | ZN513 |
D | ZN514 |
D | HOH5096 |
D | HOH5158 |
D | HOH6411 |
D | HOH6715 |
Functional Information from PROSITE/UniProt
site_id | PS00123 |
Number of Residues | 9 |
Details | ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VtDSAASAT |
Chain | Residue | Details |
A | VAL99-THR107 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Phosphoserine intermediate |
Chain | Residue | Details |
A | SER102 | |
B | SER102 | |
C | SER102 | |
D | SER102 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP51 | |
B | ASP51 | |
B | ASP153 | |
B | THR155 | |
B | GLU322 | |
B | ASP327 | |
B | HIS331 | |
B | ASP369 | |
B | HIS370 | |
B | HIS412 | |
C | ASP51 | |
A | ASP153 | |
C | ASP153 | |
C | THR155 | |
C | GLU322 | |
C | ASP327 | |
C | HIS331 | |
C | ASP369 | |
C | HIS370 | |
C | HIS412 | |
D | ASP51 | |
D | ASP153 | |
A | THR155 | |
D | THR155 | |
D | GLU322 | |
D | ASP327 | |
D | HIS331 | |
D | ASP369 | |
D | HIS370 | |
D | HIS412 | |
A | GLU322 | |
A | ASP327 | |
A | HIS331 | |
A | ASP369 | |
A | HIS370 | |
A | HIS412 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
A | ASP51 | metal ligand |
A | ASP369 | metal ligand |
A | HIS370 | metal ligand |
A | HIS412 | metal ligand |
A | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ASP153 | metal ligand |
A | THR155 | metal ligand |
A | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
A | GLU322 | metal ligand |
A | ASP327 | metal ligand |
A | LYS328 | metal ligand |
A | HIS331 | metal ligand |
site_id | MCSA2 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
B | ASP51 | metal ligand |
B | ASP369 | metal ligand |
B | HIS370 | metal ligand |
B | HIS412 | metal ligand |
B | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ASP153 | metal ligand |
B | THR155 | metal ligand |
B | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
B | GLU322 | metal ligand |
B | ASP327 | metal ligand |
B | LYS328 | metal ligand |
B | HIS331 | metal ligand |
site_id | MCSA3 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
C | ASP51 | metal ligand |
C | ASP369 | metal ligand |
C | HIS370 | metal ligand |
C | HIS412 | metal ligand |
C | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
C | ASP153 | metal ligand |
C | THR155 | metal ligand |
C | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
C | GLU322 | metal ligand |
C | ASP327 | metal ligand |
C | LYS328 | metal ligand |
C | HIS331 | metal ligand |
site_id | MCSA4 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
D | ASP51 | metal ligand |
D | ASP369 | metal ligand |
D | HIS370 | metal ligand |
D | HIS412 | metal ligand |
D | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
D | ASP153 | metal ligand |
D | THR155 | metal ligand |
D | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
D | GLU322 | metal ligand |
D | ASP327 | metal ligand |
D | LYS328 | metal ligand |
D | HIS331 | metal ligand |