4NI1
Quaternary R CO-liganded hemoglobin structure in complex with a thiol containing compound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005829 | cellular_component | cytosol |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0006954 | biological_process | inflammatory response |
| A | 0015670 | biological_process | carbon dioxide transport |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016020 | cellular_component | membrane |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0030185 | biological_process | nitric oxide transport |
| A | 0031720 | molecular_function | haptoglobin binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048821 | biological_process | erythrocyte development |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071682 | cellular_component | endocytic vesicle lumen |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005829 | cellular_component | cytosol |
| B | 0005833 | cellular_component | hemoglobin complex |
| B | 0006954 | biological_process | inflammatory response |
| B | 0008217 | biological_process | regulation of blood pressure |
| B | 0015670 | biological_process | carbon dioxide transport |
| B | 0015671 | biological_process | oxygen transport |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0030185 | biological_process | nitric oxide transport |
| B | 0030492 | molecular_function | hemoglobin binding |
| B | 0031720 | molecular_function | haptoglobin binding |
| B | 0031721 | molecular_function | hemoglobin alpha binding |
| B | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0045429 | biological_process | positive regulation of nitric oxide biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048821 | biological_process | erythrocyte development |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070293 | biological_process | renal absorption |
| B | 0070527 | biological_process | platelet aggregation |
| B | 0071682 | cellular_component | endocytic vesicle lumen |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0097746 | biological_process | blood vessel diameter maintenance |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO A 201 |
| Chain | Residue |
| A | HIS58 |
| A | VAL62 |
| A | HEM202 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 202 |
| Chain | Residue |
| A | ALA65 |
| A | LEU83 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO201 |
| A | HOH311 |
| A | HOH378 |
| A | HOH394 |
| A | TYR42 |
| A | PHE43 |
| A | HIS45 |
| A | PHE46 |
| A | HIS58 |
| A | LYS61 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2JX A 203 |
| Chain | Residue |
| A | PRO95 |
| A | LYS99 |
| A | SER102 |
| A | HIS103 |
| A | ASP126 |
| A | 2JX204 |
| A | 2JX204 |
| A | HOH318 |
| A | HOH351 |
| A | HOH371 |
| A | HOH411 |
| B | TYR35 |
| B | TRP37 |
| B | 2JX204 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 2JX A 204 |
| Chain | Residue |
| A | PRO95 |
| A | PHE98 |
| A | LYS99 |
| A | ALA130 |
| A | SER133 |
| A | THR137 |
| A | ARG141 |
| A | 2JX203 |
| A | 2JX203 |
| A | HOH301 |
| A | HOH301 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MBN A 205 |
| Chain | Residue |
| A | ALA21 |
| A | LEU66 |
| A | LEU105 |
| A | LEU109 |
| A | MBN206 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MBN A 206 |
| Chain | Residue |
| A | ALA13 |
| A | TRP14 |
| A | THR67 |
| A | VAL70 |
| A | LEU109 |
| A | MBN205 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO B 201 |
| Chain | Residue |
| B | HIS63 |
| B | VAL67 |
| B | HEM202 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 202 |
| Chain | Residue |
| A | SER3 |
| A | PRO4 |
| B | THR38 |
| B | PHE41 |
| B | PHE42 |
| B | HIS63 |
| B | ALA70 |
| B | LEU88 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU141 |
| B | CMO201 |
| B | HOH328 |
| B | HOH356 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2JX B 203 |
| Chain | Residue |
| A | SER35 |
| B | CYS93 |
| B | PRO100 |
| B | ALA142 |
| B | HOH304 |
| B | HOH306 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 2JX B 204 |
| Chain | Residue |
| A | LEU100 |
| A | HIS103 |
| A | LEU106 |
| A | HIS122 |
| A | 2JX203 |
| B | TYR35 |
| B | GLU101 |
| B | LEU105 |
| B | ASN108 |
| B | CYS112 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Peptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 140 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by N.americanus apr-2","evidences":[{"source":"PubMed","id":"12552433","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 9 |
| Details | Peptide: {"description":"LVV-hemorphin-7","featureId":"PRO_0000296641"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | Peptide: {"description":"Spinorphin","featureId":"PRO_0000424226"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"distal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-pyruvate 2-iminyl-valine; in Hb A1b"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"8637569","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843411","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) valine; in Hb A1c","evidences":[{"source":"PubMed","id":"635569","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
