3CMM
Crystal Structure of the Uba1-Ubiquitin Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004839 | molecular_function | ubiquitin activating enzyme activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
A | 0006974 | biological_process | DNA damage response |
A | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
A | 0016567 | biological_process | protein ubiquitination |
A | 0016874 | molecular_function | ligase activity |
A | 0036211 | biological_process | protein modification process |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004839 | molecular_function | ubiquitin activating enzyme activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
C | 0006974 | biological_process | DNA damage response |
C | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
C | 0016567 | biological_process | protein ubiquitination |
C | 0016874 | molecular_function | ligase activity |
C | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PRO A 5119 |
Chain | Residue |
A | ASP316 |
A | ASN320 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PRO C 5129 |
Chain | Residue |
C | ASP316 |
C | ASN320 |
C | ILE323 |
C | LYS349 |
Functional Information from PROSITE/UniProt
site_id | PS00536 |
Number of Residues | 9 |
Details | UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFtP |
Chain | Residue | Details |
A | LYS376-PRO384 |
site_id | PS00865 |
Number of Residues | 9 |
Details | UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PLCTLRsFP |
Chain | Residue | Details |
A | PRO598-PRO606 |
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KskIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG47 |
Chain | Residue | Details |
B | LYS6 | |
D | LYS29 | |
D | LYS33 | |
D | LYS63 | |
B | LYS11 | |
B | LYS27 | |
B | LYS29 | |
B | LYS33 | |
B | LYS63 | |
D | LYS6 | |
D | LYS11 | |
D | LYS27 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214 |
Chain | Residue | Details |
A | ALA444 | |
C | ASP544 | |
B | GLY76 | |
A | ARG481 | |
D | GLY76 | |
A | ASP544 | |
C | ALA444 | |
C | ASP470 | |
C | ARG481 | |
C | LYS494 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:7862120 |
Chain | Residue | Details |
B | LYS48 | |
D | LYS48 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER914 | |
C | SER914 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | LYS595 | |
A | LYS608 | |
C | LYS595 | |
C | LYS608 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 307 |
Chain | Residue | Details |
A | ARG21 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | ARG481 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | ASP544 | steric role |
A | CYS600 | activator, covalently attached, hydrogen bond donor, nucleophile, proton donor |
A | THR601 | hydrogen bond acceptor, hydrogen bond donor, increase acidity, increase nucleophilicity, proton acceptor, proton donor, proton relay |
A | ARG603 | electrostatic stabiliser, hydrogen bond donor |
A | ASN781 | electrostatic stabiliser, hydrogen bond donor |
A | ASP782 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 939 |
Chain | Residue | Details |
A | CYS600 | nucleofuge |
A | THR601 | modifies pKa |
A | ARG603 | electrostatic stabiliser |
A | ASN781 | electrostatic stabiliser |
A | ASP782 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 307 |
Chain | Residue | Details |
C | ARG21 | electrostatic stabiliser, hydrogen bond donor, steric role |
C | ARG481 | electrostatic stabiliser, hydrogen bond donor, steric role |
C | ASP544 | steric role |
C | CYS600 | activator, covalently attached, hydrogen bond donor, nucleophile, proton donor |
C | THR601 | hydrogen bond acceptor, hydrogen bond donor, increase acidity, increase nucleophilicity, proton acceptor, proton donor, proton relay |
C | ARG603 | electrostatic stabiliser, hydrogen bond donor |
C | ASN781 | electrostatic stabiliser, hydrogen bond donor |
C | ASP782 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 939 |
Chain | Residue | Details |
C | CYS600 | nucleofuge |
C | THR601 | modifies pKa |
C | ARG603 | electrostatic stabiliser |
C | ASN781 | electrostatic stabiliser |
C | ASP782 | electrostatic stabiliser |