3T1I
Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004520 | molecular_function | DNA endonuclease activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006302 | biological_process | double-strand break repair |
| A | 0008296 | molecular_function | 3'-5'-DNA exonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030870 | cellular_component | Mre11 complex |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004520 | molecular_function | DNA endonuclease activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006302 | biological_process | double-strand break repair |
| B | 0008296 | molecular_function | 3'-5'-DNA exonuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030870 | cellular_component | Mre11 complex |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004520 | molecular_function | DNA endonuclease activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006302 | biological_process | double-strand break repair |
| C | 0008296 | molecular_function | 3'-5'-DNA exonuclease activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0030870 | cellular_component | Mre11 complex |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004520 | molecular_function | DNA endonuclease activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006302 | biological_process | double-strand break repair |
| D | 0008296 | molecular_function | 3'-5'-DNA exonuclease activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0030870 | cellular_component | Mre11 complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 412 |
| Chain | Residue |
| A | ASP20 |
| A | HIS22 |
| A | ASP60 |
| A | HIS247 |
| A | MN413 |
| A | HOH504 |
| A | HOH519 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 413 |
| Chain | Residue |
| A | HIS217 |
| A | HIS245 |
| A | MN412 |
| A | HOH519 |
| A | ASP60 |
| A | ASN128 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DTT A 451 |
| Chain | Residue |
| A | ARG69 |
| A | GOL453 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DTT A 452 |
| Chain | Residue |
| A | LYS250 |
| A | ILE251 |
| A | ALA252 |
| A | HIS283 |
| A | LYS298 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 453 |
| Chain | Residue |
| A | CYS146 |
| A | DTT451 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 454 |
| Chain | Residue |
| A | ASN128 |
| A | HIS129 |
| A | HOH518 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 455 |
| Chain | Residue |
| A | PHE37 |
| A | HOH513 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 456 |
| Chain | Residue |
| A | PHE193 |
| A | LYS196 |
| A | PHE233 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 457 |
| Chain | Residue |
| A | HIS302 |
| A | GLY353 |
| A | HIS356 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 458 |
| Chain | Residue |
| A | GLN90 |
| A | GLU92 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 412 |
| Chain | Residue |
| B | ASP20 |
| B | HIS22 |
| B | ASP60 |
| B | HIS247 |
| B | MN413 |
| B | HOH507 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 413 |
| Chain | Residue |
| B | ASP60 |
| B | ASN128 |
| B | HIS217 |
| B | HIS245 |
| B | MN412 |
| B | HOH507 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 412 |
| Chain | Residue |
| C | ASP20 |
| C | HIS22 |
| C | ASP60 |
| C | HIS247 |
| C | MN413 |
| C | HOH509 |
| C | HOH520 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 413 |
| Chain | Residue |
| C | ASP60 |
| C | ASN128 |
| C | HIS217 |
| C | HIS245 |
| C | MN412 |
| C | HOH509 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 451 |
| Chain | Residue |
| C | SER98 |
| C | SER145 |
| C | GLY148 |
| C | VAL150 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 452 |
| Chain | Residue |
| C | PHE193 |
| C | VAL194 |
| C | LYS196 |
| C | PHE233 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 453 |
| Chain | Residue |
| C | GLU278 |
| C | ALA279 |
| C | VAL280 |
| C | GLN306 |
| C | PHE307 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 454 |
| Chain | Residue |
| C | SER145 |
| C | CYS146 |
| C | HOH508 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 455 |
| Chain | Residue |
| C | MSE26 |
| C | ARG32 |
| C | THR272 |
| C | LEU274 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 456 |
| Chain | Residue |
| C | ASN219 |
| C | HIS245 |
| C | GLU246 |
| C | HIS247 |
| C | HOH506 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 412 |
| Chain | Residue |
| D | ASP20 |
| D | HIS22 |
| D | ASP60 |
| D | HIS247 |
| D | MN413 |
| D | HOH504 |
| D | HOH508 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 413 |
| Chain | Residue |
| D | ASP20 |
| D | ASP60 |
| D | ASN128 |
| D | HIS217 |
| D | HIS245 |
| D | MN412 |
| D | HOH504 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL D 451 |
| Chain | Residue |
| D | ASN128 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 452 |
| Chain | Residue |
| D | PRO166 |
| D | LEU168 |
| D | LYS204 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 453 |
| Chain | Residue |
| D | ASN34 |
| D | LEU78 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q61216 |
| Chain | Residue | Details |
| A | HIS129 | |
| B | HIS129 | |
| C | HIS129 | |
| D | HIS129 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22078559, ECO:0000269|PubMed:36577401, ECO:0007744|PDB:3T1I, ECO:0007744|PDB:8BAH |
| Chain | Residue | Details |
| A | ASP20 | |
| B | ASP60 | |
| B | ASN128 | |
| B | HIS217 | |
| B | HIS245 | |
| B | HIS247 | |
| C | ASP20 | |
| C | HIS22 | |
| C | ASP60 | |
| C | ASN128 | |
| C | HIS217 | |
| A | HIS22 | |
| C | HIS245 | |
| C | HIS247 | |
| D | ASP20 | |
| D | HIS22 | |
| D | ASP60 | |
| D | ASN128 | |
| D | HIS217 | |
| D | HIS245 | |
| D | HIS247 | |
| A | ASP60 | |
| A | ASN128 | |
| A | HIS217 | |
| A | HIS245 | |
| A | HIS247 | |
| B | ASP20 | |
| B | HIS22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q61216 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| C | SER2 | |
| D | SER2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER275 | |
| B | SER275 | |
| C | SER275 | |
| D | SER275 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000269|PubMed:36050397, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS255 | |
| B | LYS255 | |
| C | LYS255 | |
| D | LYS255 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:36050397 |
| Chain | Residue | Details |
| A | LYS384 | |
| B | LYS384 | |
| C | LYS384 | |
| D | LYS384 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1) |
| Chain | Residue | Details |
| A | LYS282 | |
| B | LYS282 | |
| C | LYS282 | |
| D | LYS282 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36563124 |
| Chain | Residue | Details |
| A | LYS339 | |
| B | LYS339 | |
| C | LYS339 | |
| D | LYS339 |
