6VUA
X-ray structure of human CD38 catalytic domain with 2'-Cl-araNAD+
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue ROJ A 401 |
| Chain | Residue |
| A | TRP125 |
| A | SER186 |
| A | TRP189 |
| A | SER193 |
| A | SER220 |
| A | THR221 |
| A | PHE222 |
| A | GLU226 |
| A | HOH503 |
| A | HOH521 |
| A | HOH563 |
| A | SER126 |
| A | HOH578 |
| A | HOH596 |
| A | HOH598 |
| A | HOH599 |
| A | HOH673 |
| A | HOH682 |
| A | ARG127 |
| A | LYS129 |
| A | GLU146 |
| A | ASP155 |
| A | ASP156 |
| A | ARG177 |
| A | LYS178 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | PRO232 |
| A | VAL235 |
| A | ASN270 |
| A | HOH602 |
| A | HOH718 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue PO4 A 403 |
| Chain | Residue |
| A | CYS180 |
| A | SER181 |
| A | ARG212 |
| A | SER213 |
| A | HOH509 |
| A | HOH514 |
| A | HOH561 |
| A | HOH658 |
| A | HOH667 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | PRO60 |
| A | GLN83 |
| A | TRP86 |
| A | ASP87 |
| A | LYS90 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 405 |
| Chain | Residue |
| A | MET110 |
| A | THR114 |
| A | GLN115 |
| A | THR148 |
| A | VAL192 |
| A | PHE196 |
| A | HOH567 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue PGE A 406 |
| Chain | Residue |
| A | HIS74 |
| A | THR136 |
| A | GLN137 |
| A | ARG140 |
| A | MET142 |
| A | PHE143 |
| A | ASP147 |
| A | HOH618 |
| A | HOH690 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue PEG A 407 |
| Chain | Residue |
| A | THR56 |
| A | LYS57 |
| A | ASP156 |
| A | HOH562 |
| A | HOH574 |
| A | HOH665 |
| B | LYS57 |
| B | ARG58 |
| B | HOH557 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | PRO232 |
| B | VAL235 |
| B | ASN270 |
| B | HOH565 |
| B | HOH677 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 B 403 |
| Chain | Residue |
| B | CYS180 |
| B | SER181 |
| B | ARG212 |
| B | SER213 |
| B | HOH504 |
| B | HOH510 |
| B | HOH574 |
| B | HOH595 |
| B | HOH618 |
| B | HOH620 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 404 |
| Chain | Residue |
| B | MET110 |
| B | GLY113 |
| B | THR114 |
| B | GLN115 |
| B | HOH532 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 405 |
| Chain | Residue |
| B | PRO118 |
| B | ARG140 |
| B | ASP141 |
| B | PHE143 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 406 |
| Chain | Residue |
| B | GLN49 |
| B | TRP50 |
| B | GLY52 |
| B | GLN171 |
| B | SER172 |
| B | PEG408 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 407 |
| Chain | Residue |
| A | LYS69 |
| B | GLN83 |
| B | TRP86 |
| B | LYS90 |
| B | HOH626 |
| B | HOH630 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 408 |
| Chain | Residue |
| A | HOH554 |
| B | LYS57 |
| B | PEG406 |
| B | HOH556 |
| B | HOH664 |
| site_id | AD6 |
| Number of Residues | 31 |
| Details | binding site for Di-peptide ROJ B 401 and GLU B 226 |
| Chain | Residue |
| B | LEU124 |
| B | TRP125 |
| B | SER126 |
| B | ARG127 |
| B | LYS129 |
| B | GLU146 |
| B | ASP155 |
| B | ASP156 |
| B | ARG177 |
| B | LYS178 |
| B | SER186 |
| B | TRP189 |
| B | SER193 |
| B | ALA197 |
| B | SER220 |
| B | THR221 |
| B | PHE222 |
| B | VAL225 |
| B | VAL227 |
| B | HIS228 |
| B | ASN229 |
| B | LEU230 |
| B | HOH511 |
| B | HOH547 |
| B | HOH549 |
| B | HOH560 |
| B | HOH583 |
| B | HOH584 |
| B | HOH607 |
| B | HOH623 |
| B | HOH644 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7961800","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
