1F9B
MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 690 |
| Chain | Residue |
| A | ASP60 |
| A | TYR92 |
| A | TYR192 |
| A | HIS253 |
| A | BCT692 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 691 |
| Chain | Residue |
| A | BCT693 |
| A | ASP395 |
| A | TYR433 |
| A | TYR526 |
| A | HIS595 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT A 692 |
| Chain | Residue |
| A | ASP60 |
| A | TYR92 |
| A | THR117 |
| A | ARG121 |
| A | ALA123 |
| A | GLY124 |
| A | TYR192 |
| A | HIS253 |
| A | FE690 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT A 693 |
| Chain | Residue |
| A | ASP395 |
| A | TYR433 |
| A | THR459 |
| A | ARG463 |
| A | THR464 |
| A | ALA465 |
| A | ALA466 |
| A | TYR526 |
| A | FE691 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 3ID A 694 |
| Chain | Residue |
| A | TRP8 |
| A | CYS9 |
| A | THR10 |
| A | ILE11 |
| A | GLU15 |
| A | VAL57 |
| A | THR58 |
| A | LEU299 |
| A | PHE300 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 3ID A 695 |
| Chain | Residue |
| A | VAL350 |
| A | GLU354 |
| A | ARG463 |
| A | SER519 |
| A | TYR524 |
| A | GLY525 |
| A | LYS637 |
| A | ASN638 |
| A | HOH696 |
| A | HOH709 |
| A | HOH730 |
| A | HOH740 |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG |
| Chain | Residue | Details |
| A | TYR92-GLY101 | |
| A | TYR433-SER442 |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLengaGDVAF |
| Chain | Residue | Details |
| A | TYR192-PHE208 | |
| A | TYR526-PHE542 |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV |
| Chain | Residue | Details |
| A | LYS226-VAL256 | |
| A | ASP568-VAL598 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 327 |
| Details | Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 329 |
| Details | Domain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10366507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11599026","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution.","authors":["Mir R.","Kaur A.","Singh A.K.","Singh N.","Kaur P.","Sharma S.","Singh T.P."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10366507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531475","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution.","authors":["Mir R.","Kaur A.","Singh A.K.","Singh N.","Kaur P.","Sharma S.","Singh T.P."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
