4NTM
QueD soaked with sepiapterin (selenomethionine substituted protein)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008616 | biological_process | queuosine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008616 | biological_process | queuosine biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008616 | biological_process | queuosine biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008616 | biological_process | queuosine biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
E | 0008270 | molecular_function | zinc ion binding |
E | 0008616 | biological_process | queuosine biosynthetic process |
E | 0016829 | molecular_function | lyase activity |
E | 0042802 | molecular_function | identical protein binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
F | 0008270 | molecular_function | zinc ion binding |
F | 0008616 | biological_process | queuosine biosynthetic process |
F | 0016829 | molecular_function | lyase activity |
F | 0042802 | molecular_function | identical protein binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 201 |
Chain | Residue |
A | HIS16 |
A | HIS31 |
A | HIS33 |
A | 2K8202 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2K8 A 202 |
Chain | Residue |
A | GLU86 |
A | GLU110 |
A | ZN201 |
C | HIS71 |
E | TRP51 |
E | ILE53 |
E | ASP54 |
E | PHE55 |
A | HIS16 |
A | HIS31 |
A | HIS33 |
A | THR84 |
A | SER85 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 201 |
Chain | Residue |
B | HIS16 |
B | HIS31 |
B | HIS33 |
B | GLU110 |
B | 2K8202 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 2K8 B 202 |
Chain | Residue |
A | LEU6 |
A | TRP51 |
A | ILE53 |
A | ASP54 |
A | PHE55 |
B | HIS16 |
B | CYS27 |
B | HIS31 |
B | HIS33 |
B | THR84 |
B | SER85 |
B | GLU86 |
B | GLU110 |
B | ZN201 |
B | HOH332 |
D | HIS71 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 201 |
Chain | Residue |
C | HIS16 |
C | HIS31 |
C | HIS33 |
C | 2K8202 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 2K8 C 202 |
Chain | Residue |
A | HIS71 |
C | HIS16 |
C | LEU18 |
C | CYS27 |
C | HIS31 |
C | HIS33 |
C | THR84 |
C | SER85 |
C | GLU86 |
C | GLU110 |
C | ZN201 |
D | LEU6 |
D | TRP51 |
D | ILE53 |
D | ASP54 |
D | PHE55 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 201 |
Chain | Residue |
D | HIS16 |
D | HIS31 |
D | HIS33 |
D | GLU110 |
D | 2K8202 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2K8 D 202 |
Chain | Residue |
B | HIS71 |
D | HIS16 |
D | CYS27 |
D | HIS31 |
D | THR84 |
D | SER85 |
D | GLU86 |
D | GLU110 |
D | ZN201 |
F | LEU6 |
F | TRP51 |
F | ILE53 |
F | ASP54 |
F | PHE55 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 201 |
Chain | Residue |
E | HIS16 |
E | HIS31 |
E | HIS33 |
E | GLU110 |
E | 2K8202 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 2K8 E 202 |
Chain | Residue |
B | LEU6 |
B | TRP51 |
B | ILE53 |
B | ASP54 |
B | PHE55 |
E | HIS16 |
E | CYS27 |
E | HIS31 |
E | HIS33 |
E | THR84 |
E | SER85 |
E | GLU86 |
E | GLU110 |
E | ZN201 |
F | HIS71 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 201 |
Chain | Residue |
F | HIS33 |
F | GLU110 |
F | 2K8202 |
F | HIS16 |
F | HIS31 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 2K8 F 202 |
Chain | Residue |
C | LEU6 |
C | TRP51 |
C | ILE53 |
C | ASP54 |
C | PHE55 |
E | HIS71 |
F | HIS16 |
F | CYS27 |
F | HIS31 |
F | HIS33 |
F | THR84 |
F | SER85 |
F | GLU86 |
F | GLU110 |
F | ZN201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | CYS27 | |
B | CYS27 | |
C | CYS27 | |
D | CYS27 | |
E | CYS27 | |
F | CYS27 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | ACT_SITE: Charge relay system => ECO:0000250 |
Chain | Residue | Details |
A | HIS71 | |
E | GLU110 | |
F | HIS71 | |
F | GLU110 | |
A | GLU110 | |
B | HIS71 | |
B | GLU110 | |
C | HIS71 | |
C | GLU110 | |
D | HIS71 | |
D | GLU110 | |
E | HIS71 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS16 | |
D | HIS16 | |
D | HIS31 | |
D | HIS33 | |
E | HIS16 | |
E | HIS31 | |
E | HIS33 | |
F | HIS16 | |
F | HIS31 | |
F | HIS33 | |
A | HIS31 | |
A | HIS33 | |
B | HIS16 | |
B | HIS31 | |
B | HIS33 | |
C | HIS16 | |
C | HIS31 | |
C | HIS33 |