6FGE
Crystal structure of human ZUFSP/ZUP1 in complex with ubiquitin
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue MLI A 601 |
Chain | Residue |
A | GLN489 |
A | HIS545 |
A | LYS546 |
A | EDO603 |
A | HOH716 |
A | HOH732 |
A | HOH760 |
C | ARG42 |
C | GLN49 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 602 |
Chain | Residue |
A | TYR430 |
A | HIS441 |
A | ILE442 |
A | THR573 |
A | HOH723 |
A | HOH751 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | LEU310 |
A | PHE312 |
A | LYS544 |
A | HIS545 |
A | LYS546 |
A | MLI601 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue EDO A 604 |
Chain | Residue |
A | PHE445 |
A | HIS446 |
A | LYS447 |
A | THR449 |
A | HIS455 |
A | ARG457 |
A | LEU458 |
A | ILE577 |
A | PRO578 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | TYR275 |
A | MET304 |
A | SER307 |
A | LEU308 |
A | ASP313 |
A | ASP314 |
A | HOH774 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 606 |
Chain | Residue |
A | GLY384 |
A | LEU386 |
A | SER448 |
A | HOH713 |
A | HOH745 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue FMT A 607 |
Chain | Residue |
A | TRP423 |
A | GLY490 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue FMT A 608 |
Chain | Residue |
A | PRO451 |
A | MET540 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue FMT A 609 |
Chain | Residue |
A | LYS356 |
A | GLY357 |
A | NH4614 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue FMT A 610 |
Chain | Residue |
A | HIS446 |
A | LYS546 |
A | GLN547 |
A | HOH732 |
C | ASP39 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue FMT A 611 |
Chain | Residue |
A | ASP399 |
A | LYS402 |
A | GLU403 |
C | LYS48 |
C | ASP58 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue FMT A 612 |
Chain | Residue |
A | GLY311 |
A | MET385 |
A | LEU386 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue PEG A 613 |
Chain | Residue |
A | LYS534 |
A | ARG537 |
A | SER539 |
A | ASN542 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue NH4 A 614 |
Chain | Residue |
A | SER351 |
A | CYS360 |
A | FMT609 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue NH4 A 615 |
Chain | Residue |
A | SER351 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue ACT C 101 |
Chain | Residue |
A | LEU413 |
A | HOH803 |
C | LEU71 |
C | ARG74 |
C | HOH206 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue FMT C 102 |
Chain | Residue |
A | CYS427 |
C | ARG72 |
C | HOH224 |
C | HOH229 |
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
C | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | Region: {"description":"zUBD/ZHA","evidences":[{"source":"PubMed","id":"29476094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29576527","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"29476094","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"29476094","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q99K23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"source":"PubMed","id":"29576527","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |