1IRE
Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0018822 | molecular_function | nitrile hydratase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0050899 | biological_process | nitrile catabolic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0018822 | molecular_function | nitrile hydratase activity |
| B | 0046914 | molecular_function | transition metal ion binding |
| B | 0050899 | biological_process | nitrile catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 301 |
| Chain | Residue |
| A | CYS108 |
| A | CSD111 |
| A | SER112 |
| A | CSO113 |
| A | HOH432 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24383915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38677005","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11700034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14717710","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24383915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35919716","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Effects of arginine residue around the substrate pocket on the substrate specificity of thiocyanate hydrolase.","authors":["Yamanaka Y.","Sato M.","Arakawa T.","Namima S.","Hori S.","Ohtaki A.","Noguchi K.","Katayama Y.","Yohda M.","Odaka M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2023","submissionDatabase":"PDB data bank","title":"Crystal structure of Co-type nitrile hydratase mutant L6T from Pseudomonas thermophila at 2.2 Angstroms resolution.","authors":["Cheng Z.Y.","Ma D.","Yin M.","Lai Q.P.","Peplowski L.","Han L.C.","Hou X.D.","Yin D.J.","Rao Y.J.","Zhou Z.M."]}},{"source":"PDB","id":"1IRE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UGP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UGS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VYH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OB0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OB1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OB2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7W8L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7W8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8I6N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"11700034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14717710","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24383915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35919716","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38677005","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39447484","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Effects of arginine residue around the substrate pocket on the substrate specificity of thiocyanate hydrolase.","authors":["Yamanaka Y.","Sato M.","Arakawa T.","Namima S.","Hori S.","Ohtaki A.","Noguchi K.","Katayama Y.","Yohda M.","Odaka M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2023","submissionDatabase":"PDB data bank","title":"Crystal structure of Co-type nitrile hydratase mutant L6T from Pseudomonas thermophila at 2.2 Angstroms resolution.","authors":["Cheng Z.Y.","Ma D.","Yin M.","Lai Q.P.","Peplowski L.","Han L.C.","Hou X.D.","Yin D.J.","Rao Y.J.","Zhou Z.M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"11700034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14717710","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24383915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35919716","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38677005","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39447484","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Effects of arginine residue around the substrate pocket on the substrate specificity of thiocyanate hydrolase.","authors":["Yamanaka Y.","Sato M.","Arakawa T.","Namima S.","Hori S.","Ohtaki A.","Noguchi K.","Katayama Y.","Yohda M.","Odaka M."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2023","submissionDatabase":"PDB data bank","title":"Crystal structure of Co-type nitrile hydratase mutant L6T from Pseudomonas thermophila at 2.2 Angstroms resolution.","authors":["Cheng Z.Y.","Ma D.","Yin M.","Lai Q.P.","Peplowski L.","Han L.C.","Hou X.D.","Yin D.J.","Rao Y.J.","Zhou Z.M."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ahj |
| Chain | Residue | Details |
| A | CSD111 | |
| A | CSO113 | |
| A | SER112 | |
| B | ARG52 |
