Details
Structure visualisation
Entry information
| Complex | |
| AACDB_ID: | 1600 |
| PDBID: | 5NH3 |
| Chains: | IM_B |
| Organism: | Homo sapiens |
| Method: | XRD |
| Resolution (Å): | 2.35 |
| Reference: | 10.1073/pnas.1707925114 |
| Antibody | |
| Antibody: | Bimagrumab Fv |
| Antibody mutation: | No |
| INN (Clinical Trial): | |
| Antigen | |
| Antigen: | Activin receptor type-2A |
| Antigen mutation: | No |
| Durg Target: | P27037 |
Sequence information
Antibody
Heavy Chain: I
Mutation: NULL
| >5NH3_I|Chain C[auth H], D[auth I]|anti-human ActRIIB mAb BYM338 Fv heavy-chain|Homo sapiens (9606) QVQLVQSGAEVKKPGASVKVSCKASGYTFTSSYINWVRQAPGQGLEWMGTINPVSGSTSYAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARGGWFDYWGQGTLVTVSSHHHHHH |
Light Chain: M
Mutation: NULL
| >5NH3_M|Chain E[auth L], F[auth M]|anti-human ActRIIB mAb BYM338 Fv light-chain|Homo sapiens (9606) QSALTQPASVSGSPGQSITISCTGTSSDVGSYNYVNWYQQHPGKAPKLMIYGVSKRPSGVSNRFSGSKSGNTASLTISGLQAEDEADYYCGTFAGGSYYGVFGGGTKLTVLWSHPQFEK |
Antigen
Chain: B
Mutation: NULL
| >5NH3_B|Chain A, B|Activin receptor type-2A|Homo sapiens (9606) AILGRSETQECLFFNANWEKDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPEFRHDS |
Interaction
1、Solvent accessible surface areas (SASA) were calculated (Naccess V2.1.1) for each residue in antibody and antigen, respectively. The residues with SASA loss in binding of more than 1Å2 were classified as interacting residues.
Interacting residues (ΔSASA based)
| Chain residues position delta_SASA
: residuesposition I: THR28 THR30 SER31 SER32 TYR33 ASN52 PRO53 VAL54 SER55 SER57 ARG72 THR74 SER75 ARG98 GLY100 TRP101 M: TYR32 ASN33 TYR34 TYR51 LYS55 PHE93 GLY95 GLY96 SER97 TYR98 B: ASN36 LYS39 ASP40 GLU48 ASP55 ARG58 PHE61 THR63 VAL74 LYS75 CYS78 TRP79 LEU80 ASP81 ASP82 ILE83 ASN84 TYR86 LYS95 VAL100 PHE102 |
2、We defined interacting paratope-epitope residues by a distance cutoff of < 6 Å . Two amino acids are considered as interacting residues if they have at least one atom within a distance of 6 Å from any atom.
Interacting residues (Atom distance based)
