6O5E
Crystal structure of the Vitronectin hemopexin-like domain
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 501 |
| Chain | Residue |
| A | ASP162 |
| A | ASP207 |
| A | ASP255 |
| A | ASP347 |
| A | HOH689 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | ALA257 |
| A | ALA349 |
| A | NA503 |
| A | ALA163 |
| A | PHE164 |
| A | ALA208 |
| A | ALA209 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 503 |
| Chain | Residue |
| A | PHE164 |
| A | ALA209 |
| A | ALA257 |
| A | ALA349 |
| A | CL502 |
| A | HOH621 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | TYR220 |
| A | TYR227 |
| A | ARG229 |
| A | TYR239 |
| A | PHE247 |
| A | HOH628 |
| A | HOH632 |
| A | HOH637 |
| A | HOH652 |
| B | ARG450 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue IMD A 505 |
| Chain | Residue |
| A | HOH635 |
| B | ILE354 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 501 |
| Chain | Residue |
| B | ASP162 |
| B | ASP207 |
| B | ASP255 |
| B | ASP347 |
| B | HOH664 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | ALA163 |
| B | PHE164 |
| B | ALA209 |
| B | ALA257 |
| B | ALA348 |
| B | ALA349 |
| B | NA503 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| B | PHE164 |
| B | ALA209 |
| B | ALA257 |
| B | ALA349 |
| B | CL502 |
| B | SO4504 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | PHE164 |
| B | THR165 |
| B | ASP166 |
| B | LYS168 |
| B | ALA209 |
| B | PHE210 |
| B | THR211 |
| B | ALA257 |
| B | LEU258 |
| B | ALA259 |
| B | MET350 |
| B | ALA351 |
| B | NA503 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| B | TYR220 |
| B | TYR227 |
| B | ARG229 |
| B | TYR239 |
| B | ARG241 |
| B | HOH610 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 B 506 |
| Chain | Residue |
| B | ARG446 |
| B | ARG463 |
| B | HOH618 |
Functional Information from PROSITE/UniProt
| site_id | PS00024 |
| Number of Residues | 15 |
| Details | HEMOPEXIN Hemopexin domain signature. IRdvWgi.EgPIDAAF |
| Chain | Residue | Details |
| A | ILE196-PHE210 | |
| A | ILE335-MET350 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Repeat: {"description":"Hemopexin 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 47 |
| Details | Repeat: {"description":"Hemopexin 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
