3N2N
The Crystal Structure of Tumor Endothelial Marker 8 (TEM8) extracellular domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016021 | cellular_component | integral component of membrane |
| A | 0038023 | molecular_function | signaling receptor activity |
| B | 0016021 | cellular_component | integral component of membrane |
| B | 0038023 | molecular_function | signaling receptor activity |
| C | 0016021 | cellular_component | integral component of membrane |
| C | 0038023 | molecular_function | signaling receptor activity |
| D | 0016021 | cellular_component | integral component of membrane |
| D | 0038023 | molecular_function | signaling receptor activity |
| E | 0016021 | cellular_component | integral component of membrane |
| E | 0038023 | molecular_function | signaling receptor activity |
| F | 0016021 | cellular_component | integral component of membrane |
| F | 0038023 | molecular_function | signaling receptor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT F 1 |
| Chain | Residue |
| F | SER52 |
| F | GLY53 |
| F | SER54 |
| F | GLY116 |
| F | ASP117 |
| F | THR118 |
| F | MG221 |
| F | HOH250 |
| F | HOH304 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 221 |
| Chain | Residue |
| F | ACT1 |
| F | HOH3 |
| F | SER52 |
| F | SER54 |
| F | THR118 |
| F | HOH304 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT F 222 |
| Chain | Residue |
| E | LYS51 |
| E | LEU92 |
| F | HIS154 |
| F | HOH247 |
| F | HOH273 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT F 223 |
| Chain | Residue |
| D | GLN104 |
| F | LYS72 |
| F | PHE73 |
| F | HIS213 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT F 224 |
| Chain | Residue |
| D | HIS154 |
| D | ACT221 |
| D | HOH237 |
| F | LYS51 |
| F | HOH258 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1 |
| Chain | Residue |
| A | HOH4 |
| A | SER52 |
| A | SER54 |
| A | THR118 |
| A | ACT221 |
| A | HOH313 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 221 |
| Chain | Residue |
| A | MG1 |
| A | HOH4 |
| A | SER52 |
| A | GLY53 |
| A | SER54 |
| A | GLY116 |
| A | ASP117 |
| A | THR118 |
| A | HOH238 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 222 |
| Chain | Residue |
| A | LYS51 |
| A | HOH250 |
| A | HOH848 |
| C | HIS154 |
| C | ACT221 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 223 |
| Chain | Residue |
| A | PHE73 |
| A | HIS213 |
| A | HOH484 |
| C | GLN104 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1 |
| Chain | Residue |
| B | HOH5 |
| B | SER52 |
| B | SER54 |
| B | THR118 |
| B | ACT221 |
| B | HOH329 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT B 221 |
| Chain | Residue |
| B | MG1 |
| B | HOH5 |
| B | SER52 |
| B | GLY53 |
| B | SER54 |
| B | GLY116 |
| B | ASP117 |
| B | THR118 |
| B | HOH238 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 222 |
| Chain | Residue |
| A | HIS154 |
| B | LYS51 |
| B | LEU92 |
| B | GLU108 |
| B | VAL112 |
| B | HOH286 |
| B | HOH302 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 223 |
| Chain | Residue |
| B | HIS154 |
| B | HOH330 |
| B | HOH525 |
| C | LYS51 |
| C | VAL84 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 224 |
| Chain | Residue |
| A | GLN104 |
| B | LYS72 |
| B | PHE73 |
| B | HIS213 |
| B | HOH333 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1 |
| Chain | Residue |
| C | SER52 |
| C | SER54 |
| C | THR118 |
| C | ACT221 |
| C | HOH310 |
| C | HOH314 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT C 221 |
| Chain | Residue |
| C | HOH239 |
| C | HOH310 |
| A | ACT222 |
| C | MG1 |
| C | SER52 |
| C | GLY53 |
| C | SER54 |
| C | GLY116 |
| C | ASP117 |
| C | THR118 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 222 |
| Chain | Residue |
| B | ARG103 |
| B | GLN104 |
| C | LYS72 |
| C | PHE73 |
| C | HIS213 |
| C | HOH386 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 1 |
| Chain | Residue |
| D | HOH6 |
| D | HOH9 |
| D | SER52 |
| D | SER54 |
| D | THR118 |
| D | ACT221 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT D 221 |
| Chain | Residue |
| D | MG1 |
| D | HOH9 |
| D | SER52 |
| D | GLY53 |
| D | SER54 |
| D | GLY116 |
| D | ASP117 |
| D | THR118 |
| D | HOH265 |
| F | ACT224 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 222 |
| Chain | Residue |
| D | LYS51 |
| D | VAL84 |
| D | VAL112 |
| D | HOH224 |
| D | HOH250 |
| E | HIS154 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 223 |
| Chain | Residue |
| D | PHE73 |
| D | HIS213 |
| D | HOH612 |
| D | HOH832 |
| E | ARG103 |
| E | GLN104 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 1 |
| Chain | Residue |
| E | HOH13 |
| E | SER52 |
| E | SER54 |
| E | THR118 |
| E | ACT221 |
| E | HOH309 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT E 221 |
| Chain | Residue |
| E | MG1 |
| E | SER52 |
| E | GLY53 |
| E | SER54 |
| E | GLY116 |
| E | ASP117 |
| E | THR118 |
| E | HOH237 |
| E | HOH309 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT E 222 |
| Chain | Residue |
| E | LYS72 |
| E | PHE73 |
| E | HIS213 |
| E | HOH487 |
| F | ARG103 |
| F | GLN104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20585457, ECO:0007744|PDB:3N2N |
| Chain | Residue | Details |
| F | SER52 | |
| C | SER52 | |
| C | SER54 | |
| C | THR118 | |
| D | SER52 | |
| D | SER54 | |
| D | THR118 | |
| E | SER52 | |
| E | SER54 | |
| E | THR118 | |
| F | SER54 | |
| F | THR118 | |
| A | SER52 | |
| A | SER54 | |
| A | THR118 | |
| B | SER52 | |
| B | SER54 | |
| B | THR118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| F | ASN166 | |
| A | ASN166 | |
| B | ASN166 | |
| C | ASN166 | |
| D | ASN166 | |
| E | ASN166 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| F | ASN184 | |
| A | ASN184 | |
| B | ASN184 | |
| C | ASN184 | |
| D | ASN184 | |
| E | ASN184 |
