1VCD
Crystal Structure of a T.thermophilus HB8 Ap6A hydrolase Ndx1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004081 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006167 | biological_process | AMP biosynthetic process |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004081 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006167 | biological_process | AMP biosynthetic process |
| B | 0006754 | biological_process | ATP biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
| Chain | Residue |
| B | LYS30 |
| B | TYR66 |
| B | ASN68 |
| B | ARG74 |
| B | HOH2016 |
| B | HOH2030 |
| B | HOH2045 |
| B | HOH2066 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | ASN68 |
| A | ARG74 |
| A | TYR66 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | ARG123 |
| A | HOH2074 |
| B | GLY36 |
| B | GLU41 |
| B | VAL67 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 2002 |
| Chain | Residue |
| B | ASP21 |
| B | VAL27 |
| B | PRO29 |
| B | LYS30 |
| B | GLU50 |
| B | HOH2015 |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GhpepgEsleeAAvREVwEEtG |
| Chain | Residue | Details |
| A | GLY31-GLY52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Crystal Structure of Nudix Protein Ndx1 from Thermus thermophilus HB8 in binary complex with diadenosine hexaphosphate.","authors":["Iwai T.","Nakagawa N.","Kuramitsu S.","Masui R."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15024014","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
