1ZTE
Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Suerpoxide Dismutase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004784 | molecular_function | superoxide dismutase activity |
A | 0006801 | biological_process | superoxide metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004784 | molecular_function | superoxide dismutase activity |
B | 0006801 | biological_process | superoxide metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004784 | molecular_function | superoxide dismutase activity |
C | 0006801 | biological_process | superoxide metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004784 | molecular_function | superoxide dismutase activity |
D | 0006801 | biological_process | superoxide metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 199 |
Chain | Residue |
A | HIS26 |
A | HIS74 |
A | ASP159 |
A | HIS163 |
A | HOH5011 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 199 |
Chain | Residue |
B | HOH5022 |
B | HIS26 |
B | HIS74 |
B | ASP159 |
B | HIS163 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 199 |
Chain | Residue |
C | HIS26 |
C | HIS74 |
C | ASP159 |
C | HIS163 |
C | HOH5033 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 199 |
Chain | Residue |
D | HIS26 |
D | HIS74 |
D | ASP159 |
D | HIS163 |
D | HOH5044 |
Functional Information from PROSITE/UniProt
site_id | PS00088 |
Number of Residues | 8 |
Details | SOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY |
Chain | Residue | Details |
A | ASP159-TYR166 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K |
Chain | Residue | Details |
A | HIS26 | |
C | HIS74 | |
C | ASP159 | |
C | HIS163 | |
D | HIS26 | |
D | HIS74 | |
D | ASP159 | |
D | HIS163 | |
A | HIS74 | |
A | ASP159 | |
A | HIS163 | |
B | HIS26 | |
B | HIS74 | |
B | ASP159 | |
B | HIS163 | |
C | HIS26 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855 |
Chain | Residue | Details |
A | HIS34 | |
B | HIS34 | |
C | HIS34 | |
D | HIS34 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671 |
Chain | Residue | Details |
A | LYS44 | |
C | LYS51 | |
C | LYS98 | |
C | LYS106 | |
D | LYS44 | |
D | LYS51 | |
D | LYS98 | |
D | LYS106 | |
A | LYS51 | |
A | LYS98 | |
A | LYS106 | |
B | LYS44 | |
B | LYS51 | |
B | LYS98 | |
B | LYS106 | |
C | LYS44 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09671 |
Chain | Residue | Details |
A | LYS90 | |
A | LYS178 | |
B | LYS90 | |
B | LYS178 | |
C | LYS90 | |
C | LYS178 | |
D | LYS90 | |
D | LYS178 |