1T0L
Crystal structure of human cytosolic NADP(+)-dependent isocitrate dehydrogenase in complex with NADP, isocitrate, and calcium(2+)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006739 | biological_process | NADP+ metabolic process |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0008585 | biological_process | female gonad development |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048545 | biological_process | response to steroid hormone |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006739 | biological_process | NADP+ metabolic process |
| B | 0006740 | biological_process | NADPH regeneration |
| B | 0008585 | biological_process | female gonad development |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048545 | biological_process | response to steroid hormone |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0005829 | cellular_component | cytosol |
| C | 0006097 | biological_process | glyoxylate cycle |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006102 | biological_process | isocitrate metabolic process |
| C | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| C | 0006739 | biological_process | NADP+ metabolic process |
| C | 0006740 | biological_process | NADPH regeneration |
| C | 0008585 | biological_process | female gonad development |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0034774 | cellular_component | secretory granule lumen |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0045296 | molecular_function | cadherin binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048545 | biological_process | response to steroid hormone |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 1904724 | cellular_component | tertiary granule lumen |
| C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005782 | cellular_component | peroxisomal matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0006097 | biological_process | glyoxylate cycle |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006102 | biological_process | isocitrate metabolic process |
| D | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| D | 0006739 | biological_process | NADP+ metabolic process |
| D | 0006740 | biological_process | NADPH regeneration |
| D | 0008585 | biological_process | female gonad development |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0034774 | cellular_component | secretory granule lumen |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0045296 | molecular_function | cadherin binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048545 | biological_process | response to steroid hormone |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 1904724 | cellular_component | tertiary granule lumen |
| D | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1717 |
| Chain | Residue |
| A | ARG109 |
| A | ASP275 |
| A | ASP279 |
| A | ICT1616 |
| A | HOH1763 |
| B | ASP252 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1718 |
| Chain | Residue |
| B | ICT1617 |
| B | HOH1897 |
| A | ASP252 |
| B | ASP275 |
| B | ASP279 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 1719 |
| Chain | Residue |
| C | ASP275 |
| C | ASP279 |
| C | ICT1618 |
| C | HOH1733 |
| C | HOH1859 |
| D | ASP252 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 1720 |
| Chain | Residue |
| C | ASP252 |
| D | ASP275 |
| D | ASP279 |
| D | ICT1619 |
| D | HOH1806 |
| D | HOH1815 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 1515 |
| Chain | Residue |
| A | LYS72 |
| A | ALA74 |
| A | THR75 |
| A | ILE76 |
| A | THR77 |
| A | ARG82 |
| A | ASN96 |
| A | LEU288 |
| A | ALA308 |
| A | HIS309 |
| A | GLY310 |
| A | THR311 |
| A | VAL312 |
| A | THR313 |
| A | ARG314 |
| A | HIS315 |
| A | THR327 |
| A | ASN328 |
| A | ICT1616 |
| A | HOH1718 |
| A | HOH1720 |
| A | HOH1773 |
| A | HOH1782 |
| A | HOH1807 |
| A | HOH1844 |
| A | HOH1856 |
| A | HOH1859 |
| A | HOH1914 |
| B | GLN257 |
| B | LYS260 |
| B | HOH1799 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP B 1516 |
| Chain | Residue |
| A | ASP253 |
| A | GLN257 |
| A | LYS260 |
| B | LYS72 |
| B | ALA74 |
| B | THR75 |
| B | ILE76 |
| B | THR77 |
| B | ARG82 |
| B | ASN96 |
| B | LEU288 |
| B | ALA308 |
| B | HIS309 |
| B | GLY310 |
| B | THR311 |
| B | VAL312 |
| B | THR313 |
| B | ARG314 |
| B | HIS315 |
| B | ASN328 |
| B | ICT1617 |
| B | HOH1721 |
| B | HOH1722 |
| B | HOH1737 |
| B | HOH1741 |
| B | HOH1749 |
| B | HOH1803 |
| B | HOH1872 |
| B | HOH1897 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP C 1517 |
| Chain | Residue |
| C | THR327 |
| C | ASN328 |
| C | ICT1618 |
| C | HOH1723 |
| C | HOH1727 |
| C | HOH1739 |
| C | HOH1743 |
| C | HOH1746 |
| C | HOH1793 |
| C | HOH1819 |
| C | HOH1852 |
| C | HOH1907 |
| D | ASP253 |
| D | GLN257 |
| D | LYS260 |
| C | LYS72 |
| C | ALA74 |
| C | THR75 |
| C | ILE76 |
| C | THR77 |
| C | ARG82 |
| C | ASN96 |
| C | LEU288 |
| C | ALA308 |
| C | HIS309 |
| C | GLY310 |
| C | THR311 |
| C | VAL312 |
| C | THR313 |
| C | ARG314 |
| C | HIS315 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP D 1518 |
| Chain | Residue |
| C | ASP253 |
| C | GLN257 |
| C | LYS260 |
| D | LYS72 |
| D | ALA74 |
| D | THR75 |
| D | ILE76 |
| D | THR77 |
| D | ARG82 |
| D | ASN96 |
| D | LEU288 |
| D | ALA307 |
| D | ALA308 |
| D | HIS309 |
| D | GLY310 |
| D | THR311 |
| D | VAL312 |
| D | THR313 |
| D | ARG314 |
| D | HIS315 |
| D | ASN328 |
| D | ICT1619 |
| D | HOH1748 |
| D | HOH1771 |
| D | HOH1825 |
| D | HOH1826 |
| D | HOH1922 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ICT A 1616 |
| Chain | Residue |
| A | THR77 |
| A | SER94 |
| A | ARG100 |
| A | ARG109 |
| A | ARG132 |
| A | TYR139 |
| A | ASP275 |
| A | NAP1515 |
| A | CA1717 |
| B | LYS212 |
| B | THR214 |
| B | ASP252 |
| B | HOH1886 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ICT B 1617 |
| Chain | Residue |
| A | LYS212 |
| A | THR214 |
| A | ASP252 |
| B | THR77 |
| B | SER94 |
| B | ARG100 |
| B | ARG109 |
| B | ARG132 |
| B | TYR139 |
| B | ASP275 |
| B | NAP1516 |
| B | CA1718 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ICT C 1618 |
| Chain | Residue |
| C | THR77 |
| C | SER94 |
| C | ARG100 |
| C | ARG109 |
| C | ARG132 |
| C | TYR139 |
| C | ASP275 |
| C | NAP1517 |
| C | CA1719 |
| D | LYS212 |
| D | THR214 |
| D | ILE215 |
| D | ASP252 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ICT D 1619 |
| Chain | Residue |
| C | LYS212 |
| C | THR214 |
| C | ASP252 |
| D | THR77 |
| D | SER94 |
| D | ARG100 |
| D | ARG109 |
| D | ARG132 |
| D | TYR139 |
| D | ASP275 |
| D | NAP1518 |
| D | CA1720 |
| D | HOH1767 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM |
| Chain | Residue | Details |
| A | ASN271-MET290 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XRX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L58","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TQH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XRX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TQH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Site: {"description":"Critical for catalysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | VAL146 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | THR155 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | THR155 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | THR155 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | VAL146 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | VAL146 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | VAL146 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | LYS212 | |
| A | ASP252 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | LYS212 | |
| B | ASP252 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | LYS212 | |
| C | ASP252 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | LYS212 | |
| D | ASP252 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | THR155 |
