5AUO
Crystal structure of the HypAB-Ni complex (AMPPCP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051604 | biological_process | protein maturation |
| 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 | 4 |
| Details | binding site for residue ZN A 201 |
| Chain | Residue |
| A | CYS73 |
| A | CYS76 |
| A | CYS110 |
| A | CYS113 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NI A 202 |
| Chain | Residue |
| A | MET1 |
| A | HIS2 |
| A | GLU3 |
| A | HIS98 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 203 |
| Chain | Residue |
| A | THR55 |
| A | ILE56 |
| A | GLN19 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue ACP B 301 |
| Chain | Residue |
| B | LYS28 |
| B | GLY29 |
| B | GLY29 |
| B | GLY30 |
| B | VAL31 |
| B | GLY32 |
| B | LYS33 |
| B | SER34 |
| B | LEU35 |
| B | ASP57 |
| B | PRO135 |
| B | SER160 |
| B | LEU162 |
| B | ASN187 |
| B | MET188 |
| B | PRO217 |
| B | PHE218 |
| B | TYR219 |
| B | MG302 |
| B | HOH414 |
| B | HOH436 |
| B | HOH454 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | SER34 |
| B | ACP301 |
| B | HOH422 |
| B | HOH436 |
| B | HOH454 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| A | HOH316 |
| A | HOH355 |
| B | LYS149 |
| B | HOH408 |
| B | HOH425 |
| B | HOH490 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| A | PRO111 |
| A | LYS112 |
| B | ARG79 |
Functional Information from PROSITE/UniProt
| site_id | PS01249 |
| Number of Residues | 43 |
| Details | HYPA Hydrogenases expression/synthesis hypA family signature. GelqdVaediVkfAMeqlfagTiaeg.AeIeFveeeavfkCrnC |
| Chain | Residue | Details |
| A | GLY34-CYS76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26056269","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AUO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00213","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19769985","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26056269","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A43","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A44","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AUO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AUP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
