3VX3
Crystal structure of [NiFe] hydrogenase maturation protein HypB from Thermococcus kodakarensis KOD1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0016226 | biological_process | iron-sulfur cluster assembly |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
A | 0140663 | molecular_function | ATP-dependent FeS chaperone activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0016226 | biological_process | iron-sulfur cluster assembly |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0140663 | molecular_function | ATP-dependent FeS chaperone activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | GLY30 |
A | TYR219 |
A | ASP223 |
A | HOH411 |
A | HOH414 |
A | HOH436 |
B | LYS28 |
B | SER160 |
B | LEU162 |
A | VAL31 |
A | GLY32 |
A | LYS33 |
A | SER34 |
A | LEU35 |
A | ASN187 |
A | PRO217 |
A | PHE218 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | LYS28 |
A | GLY29 |
B | LYS28 |
B | GLY29 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | ASP139 |
A | HOH473 |
B | GLY107 |
B | ILE110 |
B | ASP139 |
B | GLN140 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | GLY68 |
A | GLY227 |
A | ASN228 |
A | HOH470 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP B 301 |
Chain | Residue |
A | LYS28 |
A | SER160 |
A | LEU162 |
B | GLY29 |
B | GLY30 |
B | VAL31 |
B | GLY32 |
B | LYS33 |
B | SER34 |
B | LEU35 |
B | ASN187 |
B | MET188 |
B | PRO217 |
B | PHE218 |
B | TYR219 |
B | ASP223 |
B | VAL226 |
B | HOH408 |
B | HOH414 |
B | HOH422 |
B | HOH433 |
B | HOH443 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | TYR219 |
B | PRO220 |
B | ASP221 |
B | LEU222 |
B | LYS225 |
B | HOH415 |
B | HOH463 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | LYS175 |
B | LYS180 |
B | VAL181 |
B | GLY209 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
A | GLU176 |
B | TYR97 |
B | ALA113 |
B | GLU116 |
B | LEU117 |
B | ILE120 |