Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016874 | molecular_function | ligase activity |
A | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016874 | molecular_function | ligase activity |
B | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016874 | molecular_function | ligase activity |
C | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016874 | molecular_function | ligase activity |
D | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
E | 0000166 | molecular_function | nucleotide binding |
E | 0016874 | molecular_function | ligase activity |
E | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue AMP A 501 |
Chain | Residue |
A | GLY271 |
A | ASP377 |
A | ARG392 |
A | ARG407 |
A | EQ2502 |
A | HOH607 |
A | ALA272 |
A | PRO273 |
A | GLN292 |
A | ASN293 |
A | GLY295 |
A | THR296 |
A | GLN297 |
A | VAL319 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue EQ2 A 502 |
Chain | Residue |
A | LEU202 |
A | GLY271 |
A | ASN293 |
A | TYR294 |
A | GLY295 |
A | THR296 |
A | GLN297 |
A | ALA300 |
A | PHE301 |
A | AMP501 |
A | HOH607 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue AMP B 501 |
Chain | Residue |
B | GLY271 |
B | ALA272 |
B | PRO273 |
B | GLN292 |
B | ASN293 |
B | GLY295 |
B | GLN297 |
B | VAL319 |
B | ASP377 |
B | ARG392 |
B | ARG407 |
B | EQ2502 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue EQ2 B 502 |
Chain | Residue |
B | LEU202 |
B | GLY271 |
B | ASN293 |
B | TYR294 |
B | GLY295 |
B | THR296 |
B | ALA300 |
B | PHE301 |
B | AMP501 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue AMP C 501 |
Chain | Residue |
C | GLY271 |
C | ALA272 |
C | PRO273 |
C | GLN292 |
C | ASN293 |
C | GLY295 |
C | GLN297 |
C | VAL319 |
C | ASP377 |
C | ARG392 |
C | ARG407 |
C | EQ2502 |
C | HOH602 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue EQ2 C 502 |
Chain | Residue |
C | LEU202 |
C | GLY271 |
C | ASN293 |
C | GLY295 |
C | THR296 |
C | GLN297 |
C | ALA300 |
C | PHE301 |
C | AMP501 |
C | HOH602 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue AMP D 501 |
Chain | Residue |
D | GLY271 |
D | ALA272 |
D | GLN292 |
D | ASN293 |
D | TYR294 |
D | GLY295 |
D | GLN297 |
D | VAL319 |
D | ASP377 |
D | LEU389 |
D | ARG392 |
D | ARG407 |
D | EQ2502 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue EQ2 D 502 |
Chain | Residue |
D | LEU202 |
D | GLY271 |
D | ASN293 |
D | GLY295 |
D | THR296 |
D | ALA300 |
D | PHE301 |
D | AMP501 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for residue AMP E 501 |
Chain | Residue |
E | EQ2502 |
E | HOH607 |
E | GLY271 |
E | ALA272 |
E | PRO273 |
E | GLN292 |
E | ASN293 |
E | GLY295 |
E | THR296 |
E | ASP377 |
E | ASN403 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue EQ2 E 502 |
Chain | Residue |
E | LEU202 |
E | GLY271 |
E | ASN293 |
E | TYR294 |
E | GLY295 |
E | THR296 |
E | ALA300 |
E | PHE301 |
E | AMP501 |
Functional Information from PROSITE/UniProt
site_id | PS00455 |
Number of Residues | 12 |
Details | AMP_BINDING Putative AMP-binding domain signature. VAFTSGTTGtPK |
Chain | Residue | Details |
A | VAL155-LYS166 | |