Uniprot ID: Q02153
- Protein: Guanylate cyclase soluble subunit beta-1
- Organism: Human (Homo sapiens)
- Length: 619
- Sequence:
MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETKQDDD
Number of chains: 8
| Resolution | 3.70 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-606 (1-619), 1.00 |
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 186SER-204GLN:287VAL-301ILE:439SER-441GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
| Resolution | 3.90 Å |
|---|---|
| Residue indices (Uniprot), coverage | 1-606 (1-619), 1.00 |
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 186SER-204GLN:287VAL-301ILE:439SER-441GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.17 Å |
| Residue indices (Uniprot), coverage | 1-607 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 188GLU-203THR:287VAL-301ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
| Residue indices (Uniprot), coverage | 1-607 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 188GLU-203THR:287VAL-301ILE |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
| Residue indices (Uniprot), coverage | 1-606 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 186SER-204GLN:287VAL-301ILE:439SER-441GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.17 Å |
| Residue indices (Uniprot), coverage | 1-607 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Structural gaps | Exists |
| label_asym_ids of heme | C |
| Available structure | PDB |
| Residue indices (Uniprot), coverage | 1-608 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Structural gaps | Exists |
| label_asym_ids of heme | None |
| Available structure | PDB |
| Residue indices (Uniprot), coverage | 1-609 (1-619), 1.00 |
|---|---|
| Mutations (UniProt numbering) | None |
| Insertions | None |
| Deletions | None |
| Sequence identity to UniProt | 1.0000 |
| auth_asym_id | B |
| Missing residues | 186SER-204GLN:288GLU-300GLU |
| Structural gaps | Exists |
| label_asym_ids of heme | None |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
