5SX5
Crystal Structure of panitumumab in complex with epidermal growth factor receptor domain 3 mutant S468R.
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue SO4 K 301 |
Chain | Residue |
K | LYS39 |
K | LYS45 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue SO4 K 302 |
Chain | Residue |
K | PRO59 |
K | SER60 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 K 303 |
Chain | Residue |
K | ASP1 |
K | GLN27 |
K | HIS93 |
M | ASN473 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue GOL K 304 |
Chain | Residue |
K | SER9 |
K | PRO8 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL K 305 |
Chain | Residue |
K | THR20 |
K | THR22 |
L | SER7 |
L | PRO8 |
L | THR20 |
L | THR22 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO K 306 |
Chain | Residue |
K | GLN38 |
K | ALA84 |
K | THR85 |
K | GLU165 |
K | HOH407 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue 1PE J 301 |
Chain | Residue |
J | ILE94 |
J | TYR96 |
J | MET114 |
K | GLY41 |
K | LYS42 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO J 302 |
Chain | Residue |
J | ASN161 |
J | SER162 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue SO4 L 301 |
Chain | Residue |
L | LEU11 |
L | SER12 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue SO4 L 302 |
Chain | Residue |
L | GLN27 |
L | ASP28 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue SO4 L 303 |
Chain | Residue |
L | ARG211 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue SO4 L 304 |
Chain | Residue |
L | LYS39 |
L | LYS42 |
L | LYS45 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 L 305 |
Chain | Residue |
L | ASP1 |
L | GLN27 |
L | HIS93 |
N | ASN473 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue 1PE L 306 |
Chain | Residue |
L | SER9 |
L | GLN38 |
L | ALA84 |
L | THR85 |
L | GLY100 |
L | GLY101 |
L | LYS103 |
L | GLU165 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue GOL L 307 |
Chain | Residue |
L | SER9 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue SO4 H 301 |
Chain | Residue |
H | GLY124 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue SO4 H 302 |
Chain | Residue |
H | ASN161 |
H | SER162 |
H | ASN203 |
H | HOH402 |
L | ASP185 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue SO4 H 303 |
Chain | Residue |
H | SER121 |
H | THR122 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue 1PE H 304 |
Chain | Residue |
H | ILE94 |
H | TYR96 |
H | GLN111 |
H | GLY112 |
H | GLU154 |
H | HOH415 |
L | GLN38 |
L | LYS42 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue GOL H 305 |
Chain | Residue |
H | PRO9 |
H | GLY10 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue EDO H 306 |
Chain | Residue |
H | ASP33 |
N | GLN408 |
N | VAL417 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue SO4 N 601 |
Chain | Residue |
M | HIS359 |
N | SER474 |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVDH |
Chain | Residue | Details |
J | TYR200-HIS206 | |
K | TYR192-HIS198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10731668, ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX, ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7 |
Chain | Residue | Details |
M | ASP328 | |
N | ASP328 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10731668, ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UV7 |
Chain | Residue | Details |
M | ASN337 | |
N | ASN337 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8962717, ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP |
Chain | Residue | Details |
M | ASN389 | |
N | ASN389 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:8962717, ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7 |
Chain | Residue | Details |
M | ASP420 | |
N | ASP420 |