2DW7
Crystal structure of D-tartrate dehydratase from Bradyrhizobium japonicum complexed with Mg++ and meso-tartrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| C | 0051260 | biological_process | protein homooligomerization |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| D | 0051260 | biological_process | protein homooligomerization |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| E | 0051260 | biological_process | protein homooligomerization |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| F | 0051260 | biological_process | protein homooligomerization |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0016829 | molecular_function | lyase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| G | 0051260 | biological_process | protein homooligomerization |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0016829 | molecular_function | lyase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| H | 0051260 | biological_process | protein homooligomerization |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0016829 | molecular_function | lyase activity |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| I | 0051260 | biological_process | protein homooligomerization |
| J | 0000287 | molecular_function | magnesium ion binding |
| J | 0016829 | molecular_function | lyase activity |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| J | 0051260 | biological_process | protein homooligomerization |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0016829 | molecular_function | lyase activity |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| K | 0051260 | biological_process | protein homooligomerization |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0016829 | molecular_function | lyase activity |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| L | 0051260 | biological_process | protein homooligomerization |
| M | 0000287 | molecular_function | magnesium ion binding |
| M | 0016829 | molecular_function | lyase activity |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| M | 0051260 | biological_process | protein homooligomerization |
| N | 0000287 | molecular_function | magnesium ion binding |
| N | 0016829 | molecular_function | lyase activity |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| N | 0051260 | biological_process | protein homooligomerization |
| O | 0000287 | molecular_function | magnesium ion binding |
| O | 0016829 | molecular_function | lyase activity |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| O | 0051260 | biological_process | protein homooligomerization |
| P | 0000287 | molecular_function | magnesium ion binding |
| P | 0016829 | molecular_function | lyase activity |
| P | 0046872 | molecular_function | metal ion binding |
| P | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| P | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2001 |
| Chain | Residue |
| A | ASP213 |
| A | GLU239 |
| A | GLU240 |
| A | GLU265 |
| A | SRT1001 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | SRT1002 |
| B | ASP213 |
| B | GLU239 |
| B | GLU240 |
| B | GLU265 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 2003 |
| Chain | Residue |
| C | ASP213 |
| C | ASN215 |
| C | GLU239 |
| C | GLU240 |
| C | GLU265 |
| C | SRT1003 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 2004 |
| Chain | Residue |
| D | ASP213 |
| D | GLU239 |
| D | GLU265 |
| D | SRT1004 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 2005 |
| Chain | Residue |
| E | ASP213 |
| E | GLU239 |
| E | GLU240 |
| E | GLU265 |
| E | SRT1005 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 2006 |
| Chain | Residue |
| F | ASP213 |
| F | ASN215 |
| F | GLU239 |
| F | GLU240 |
| F | GLU265 |
| F | SRT1006 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 2007 |
| Chain | Residue |
| G | ASP213 |
| G | ASN215 |
| G | GLU239 |
| G | GLU240 |
| G | GLU265 |
| G | SRT1007 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 2008 |
| Chain | Residue |
| H | ASP213 |
| H | ASN215 |
| H | GLU239 |
| H | GLU240 |
| H | GLU265 |
| H | SRT1008 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG I 2009 |
| Chain | Residue |
| I | ASP213 |
| I | ASN215 |
| I | GLU239 |
| I | GLU240 |
| I | GLU265 |
| I | SRT1009 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG J 2010 |
| Chain | Residue |
| J | ASP213 |
| J | GLU239 |
| J | GLU240 |
| J | GLU265 |
| J | SRT1010 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG K 2011 |
| Chain | Residue |
| K | ASP213 |
| K | ASN215 |
| K | GLU239 |
| K | GLU240 |
| K | GLU265 |
| K | SRT1011 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG L 2012 |
| Chain | Residue |
| L | ASP213 |
| L | ASN215 |
| L | GLU239 |
| L | GLU240 |
| L | GLU265 |
| L | SRT1012 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG M 2013 |
| Chain | Residue |
| M | ASP213 |
| M | GLU239 |
| M | GLU240 |
| M | GLU265 |
| M | SRT1013 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG N 2014 |
| Chain | Residue |
| N | ASP213 |
| N | GLU239 |
| N | GLU265 |
| N | SRT1014 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG O 2015 |
| Chain | Residue |
| O | ASP213 |
| O | GLU239 |
| O | GLU265 |
| O | SRT1015 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG P 2016 |
| Chain | Residue |
| P | ASP213 |
| P | ASN215 |
| P | GLU239 |
| P | GLU240 |
| P | GLU265 |
| P | SRT1016 |
| site_id | BC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT A 1001 |
| Chain | Residue |
| B | LYS102 |
| A | ASN21 |
| A | PHE26 |
| A | ASN55 |
| A | TYR156 |
| A | LYS182 |
| A | LYS184 |
| A | ASP213 |
| A | ASN215 |
| A | GLU239 |
| A | GLU265 |
| A | HIS322 |
| A | GLU341 |
| A | TYR343 |
| A | MG2001 |
| site_id | BC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT B 1002 |
| Chain | Residue |
| A | LYS102 |
| B | ASN21 |
| B | PHE26 |
| B | ASN55 |
| B | TYR156 |
| B | LYS182 |
| B | LYS184 |
| B | ASP213 |
| B | ASN215 |
| B | GLU239 |
| B | GLU265 |
| B | HIS322 |
| B | GLU341 |
| B | TYR343 |
| B | MG2002 |
| site_id | CC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT C 1003 |
| Chain | Residue |
| C | ASN21 |
| C | PHE26 |
| C | ASN55 |
| C | TYR156 |
| C | LYS182 |
| C | LYS184 |
| C | ASP213 |
| C | ASN215 |
| C | GLU239 |
| C | GLU265 |
| C | HIS322 |
| C | GLU341 |
| C | TYR343 |
| C | MG2003 |
| D | LYS102 |
| site_id | CC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SRT D 1004 |
| Chain | Residue |
| C | LYS102 |
| D | ASN21 |
| D | PHE26 |
| D | ASN55 |
| D | TYR156 |
| D | LYS182 |
| D | LYS184 |
| D | ASP213 |
| D | ASN215 |
| D | GLU239 |
| D | GLU265 |
| D | HIS322 |
| D | GLU341 |
| D | TYR343 |
| D | MG2004 |
| D | HOH2022 |
| site_id | CC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT E 1005 |
| Chain | Residue |
| E | ASN21 |
| E | PHE26 |
| E | ASN55 |
| E | TYR156 |
| E | LYS182 |
| E | LYS184 |
| E | ASP213 |
| E | ASN215 |
| E | GLU239 |
| E | GLU265 |
| E | HIS322 |
| E | GLU341 |
| E | TYR343 |
| E | MG2005 |
| F | LYS102 |
| site_id | CC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT F 1006 |
| Chain | Residue |
| E | LYS102 |
| F | ASN21 |
| F | PHE26 |
| F | ASN55 |
| F | TYR156 |
| F | LYS182 |
| F | LYS184 |
| F | ASP213 |
| F | ASN215 |
| F | GLU239 |
| F | GLU265 |
| F | HIS322 |
| F | GLU341 |
| F | TYR343 |
| F | MG2006 |
| site_id | CC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT G 1007 |
| Chain | Residue |
| G | ASN21 |
| G | PHE26 |
| G | ASN55 |
| G | TYR156 |
| G | LYS182 |
| G | LYS184 |
| G | ASP213 |
| G | ASN215 |
| G | GLU239 |
| G | GLU265 |
| G | HIS322 |
| G | GLU341 |
| G | TYR343 |
| G | MG2007 |
| H | LYS102 |
| site_id | CC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT H 1008 |
| Chain | Residue |
| G | LYS102 |
| H | ASN21 |
| H | PHE26 |
| H | ASN55 |
| H | TYR156 |
| H | LYS182 |
| H | LYS184 |
| H | ASP213 |
| H | ASN215 |
| H | GLU239 |
| H | GLU265 |
| H | HIS322 |
| H | GLU341 |
| H | TYR343 |
| H | MG2008 |
| site_id | CC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT I 1009 |
| Chain | Residue |
| I | ASN21 |
| I | PHE26 |
| I | ASN55 |
| I | TYR156 |
| I | LYS182 |
| I | LYS184 |
| I | ASP213 |
| I | ASN215 |
| I | GLU239 |
| I | GLU265 |
| I | HIS322 |
| I | GLU341 |
| I | TYR343 |
| I | MG2009 |
| J | LYS102 |
| site_id | CC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT J 1010 |
| Chain | Residue |
| I | LYS102 |
| J | ASN21 |
| J | PHE26 |
| J | ASN55 |
| J | TYR156 |
| J | LYS182 |
| J | LYS184 |
| J | ASP213 |
| J | ASN215 |
| J | GLU239 |
| J | GLU265 |
| J | HIS322 |
| J | GLU341 |
| J | TYR343 |
| J | MG2010 |
| site_id | CC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SRT K 1011 |
| Chain | Residue |
| K | ASN21 |
| K | PHE26 |
| K | ASN55 |
| K | TYR156 |
| K | LYS182 |
| K | LYS184 |
| K | ASP213 |
| K | ASN215 |
| K | GLU239 |
| K | GLU265 |
| K | HIS322 |
| K | GLU341 |
| K | TYR343 |
| K | MG2011 |
| K | HOH2036 |
| L | LYS102 |
| site_id | DC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT L 1012 |
| Chain | Residue |
| K | LYS102 |
| L | ASN21 |
| L | PHE26 |
| L | ASN55 |
| L | TYR156 |
| L | LYS182 |
| L | LYS184 |
| L | ASP213 |
| L | ASN215 |
| L | GLU239 |
| L | GLU265 |
| L | HIS322 |
| L | GLU341 |
| L | TYR343 |
| L | MG2012 |
| site_id | DC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT M 1013 |
| Chain | Residue |
| M | ASN21 |
| M | PHE26 |
| M | ASN55 |
| M | TYR156 |
| M | LYS182 |
| M | LYS184 |
| M | ASP213 |
| M | ASN215 |
| M | GLU239 |
| M | GLU265 |
| M | HIS322 |
| M | GLU341 |
| M | TYR343 |
| M | MG2013 |
| N | LYS102 |
| site_id | DC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT N 1014 |
| Chain | Residue |
| M | LYS102 |
| N | ASN21 |
| N | PHE26 |
| N | ASN55 |
| N | TYR156 |
| N | LYS182 |
| N | LYS184 |
| N | ASP213 |
| N | ASN215 |
| N | GLU239 |
| N | GLU265 |
| N | HIS322 |
| N | GLU341 |
| N | TYR343 |
| N | MG2014 |
| site_id | DC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT O 1015 |
| Chain | Residue |
| O | ASN21 |
| O | PHE26 |
| O | ASN55 |
| O | TYR156 |
| O | LYS182 |
| O | LYS184 |
| O | ASP213 |
| O | ASN215 |
| O | GLU239 |
| O | GLU265 |
| O | HIS322 |
| O | GLU341 |
| O | TYR343 |
| O | MG2015 |
| P | LYS102 |
| site_id | DC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SRT P 1016 |
| Chain | Residue |
| O | LYS102 |
| P | ASN21 |
| P | PHE26 |
| P | ASN55 |
| P | TYR156 |
| P | LYS182 |
| P | LYS184 |
| P | ASP213 |
| P | ASN215 |
| P | GLU239 |
| P | GLU265 |
| P | HIS322 |
| P | GLU341 |
| P | TYR343 |
| P | MG2016 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | ACT_SITE: acceptor => ECO:0000269|PubMed:17144653 |
| Chain | Residue | Details |
| A | LYS184 | |
| B | LYS184 | |
| C | LYS184 | |
| D | LYS184 | |
| E | LYS184 | |
| F | LYS184 | |
| G | LYS184 | |
| H | LYS184 | |
| I | LYS184 | |
| J | LYS184 | |
| K | LYS184 | |
| L | LYS184 | |
| M | LYS184 | |
| N | LYS184 | |
| O | LYS184 | |
| P | LYS184 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17144653 |
| Chain | Residue | Details |
| A | HIS322 | |
| B | HIS322 | |
| C | HIS322 | |
| D | HIS322 | |
| E | HIS322 | |
| F | HIS322 | |
| G | HIS322 | |
| H | HIS322 | |
| I | HIS322 | |
| J | HIS322 | |
| K | HIS322 | |
| L | HIS322 | |
| M | HIS322 | |
| N | HIS322 | |
| O | HIS322 | |
| P | HIS322 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 144 |
| Details | BINDING: |
| Chain | Residue | Details |
| F | TYR156 | |
| F | LYS182 | |
| F | GLU239 | |
| F | GLU265 | |
| F | HIS322 | |
| F | GLU341 | |
| G | ASN21 | |
| G | ASN55 | |
| G | LYS102 | |
| G | TYR156 | |
| G | LYS182 | |
| G | GLU239 | |
| G | GLU265 | |
| G | HIS322 | |
| G | GLU341 | |
| H | ASN21 | |
| H | ASN55 | |
| H | LYS102 | |
| H | TYR156 | |
| H | LYS182 | |
| H | GLU239 | |
| H | GLU265 | |
| H | HIS322 | |
| H | GLU341 | |
| I | ASN21 | |
| I | ASN55 | |
| I | LYS102 | |
| I | TYR156 | |
| I | LYS182 | |
| I | GLU239 | |
| I | GLU265 | |
| I | HIS322 | |
| I | GLU341 | |
| J | ASN21 | |
| J | ASN55 | |
| J | LYS102 | |
| J | TYR156 | |
| J | LYS182 | |
| J | GLU239 | |
| J | GLU265 | |
| J | HIS322 | |
| J | GLU341 | |
| K | ASN21 | |
| K | ASN55 | |
| K | LYS102 | |
| K | TYR156 | |
| K | LYS182 | |
| K | GLU239 | |
| K | GLU265 | |
| K | HIS322 | |
| K | GLU341 | |
| L | ASN21 | |
| L | ASN55 | |
| L | LYS102 | |
| L | TYR156 | |
| L | LYS182 | |
| L | GLU239 | |
| L | GLU265 | |
| L | HIS322 | |
| L | GLU341 | |
| M | ASN21 | |
| M | ASN55 | |
| M | LYS102 | |
| M | TYR156 | |
| M | LYS182 | |
| M | GLU239 | |
| M | GLU265 | |
| M | HIS322 | |
| M | GLU341 | |
| N | ASN21 | |
| N | ASN55 | |
| N | LYS102 | |
| N | TYR156 | |
| N | LYS182 | |
| N | GLU239 | |
| N | GLU265 | |
| N | HIS322 | |
| N | GLU341 | |
| O | ASN21 | |
| O | ASN55 | |
| O | LYS102 | |
| O | TYR156 | |
| O | LYS182 | |
| O | GLU239 | |
| O | GLU265 | |
| O | HIS322 | |
| O | GLU341 | |
| P | ASN21 | |
| P | ASN55 | |
| P | LYS102 | |
| P | TYR156 | |
| P | LYS182 | |
| P | GLU239 | |
| P | GLU265 | |
| P | HIS322 | |
| P | GLU341 | |
| A | ASN21 | |
| A | ASN55 | |
| A | LYS102 | |
| A | TYR156 | |
| A | LYS182 | |
| A | GLU239 | |
| A | GLU265 | |
| A | HIS322 | |
| A | GLU341 | |
| B | ASN21 | |
| B | ASN55 | |
| B | LYS102 | |
| B | TYR156 | |
| B | LYS182 | |
| B | GLU239 | |
| B | GLU265 | |
| B | HIS322 | |
| B | GLU341 | |
| C | ASN21 | |
| C | ASN55 | |
| C | LYS102 | |
| C | TYR156 | |
| C | LYS182 | |
| C | GLU239 | |
| C | GLU265 | |
| C | HIS322 | |
| C | GLU341 | |
| D | ASN21 | |
| D | ASN55 | |
| D | LYS102 | |
| D | TYR156 | |
| D | LYS182 | |
| D | GLU239 | |
| D | GLU265 | |
| D | HIS322 | |
| D | GLU341 | |
| E | ASN21 | |
| E | ASN55 | |
| E | LYS102 | |
| E | TYR156 | |
| E | LYS182 | |
| E | GLU239 | |
| E | GLU265 | |
| E | HIS322 | |
| E | GLU341 | |
| F | ASN21 | |
| F | ASN55 | |
| F | LYS102 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17144653 |
| Chain | Residue | Details |
| A | ASP213 | |
| B | ASP213 | |
| C | ASP213 | |
| D | ASP213 | |
| E | ASP213 | |
| F | ASP213 | |
| G | ASP213 | |
| H | ASP213 | |
| I | ASP213 | |
| J | ASP213 | |
| K | ASP213 | |
| L | ASP213 | |
| M | ASP213 | |
| N | ASP213 | |
| O | ASP213 | |
| P | ASP213 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ASN55 | |
| A | LYS182 | |
| A | GLU341 | |
| B | ASN55 | |
| B | LYS182 | |
| B | GLU341 | |
| C | ASN55 | |
| C | LYS182 | |
| C | GLU341 | |
| D | ASN55 | |
| D | LYS182 | |
| D | GLU341 | |
| E | ASN55 | |
| E | LYS182 | |
| E | GLU341 | |
| F | ASN55 | |
| F | LYS182 | |
| F | GLU341 | |
| G | ASN55 | |
| G | LYS182 | |
| G | GLU341 | |
| H | ASN55 | |
| H | LYS182 | |
| H | GLU341 | |
| I | ASN55 | |
| I | LYS182 | |
| I | GLU341 | |
| J | ASN55 | |
| J | LYS182 | |
| J | GLU341 | |
| K | ASN55 | |
| K | LYS182 | |
| K | GLU341 | |
| L | ASN55 | |
| L | LYS182 | |
| L | GLU341 | |
| M | ASN55 | |
| M | LYS182 | |
| M | GLU341 | |
| N | ASN55 | |
| N | LYS182 | |
| N | GLU341 | |
| O | ASN55 | |
| O | LYS182 | |
| O | GLU341 | |
| P | ASN55 | |
| P | LYS182 | |
| P | GLU341 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | SITE: Increases basicity of active site His |
| Chain | Residue | Details |
| A | ASP292 | |
| B | ASP292 | |
| C | ASP292 | |
| D | ASP292 | |
| E | ASP292 | |
| F | ASP292 | |
| G | ASP292 | |
| H | ASP292 | |
| I | ASP292 | |
| J | ASP292 | |
| K | ASP292 | |
| L | ASP292 | |
| M | ASP292 | |
| N | ASP292 | |
| O | ASP292 | |
| P | ASP292 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| A | ASN55 | electrostatic stabiliser |
| A | LYS182 | electrostatic stabiliser |
| A | LYS184 | proton acceptor, proton donor |
| A | ASP213 | metal ligand |
| A | GLU239 | metal ligand |
| A | GLU265 | metal ligand |
| A | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| A | HIS322 | proton acceptor, proton donor |
| A | GLU341 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| B | ASN55 | electrostatic stabiliser |
| B | LYS182 | electrostatic stabiliser |
| B | LYS184 | proton acceptor, proton donor |
| B | ASP213 | metal ligand |
| B | GLU239 | metal ligand |
| B | GLU265 | metal ligand |
| B | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| B | HIS322 | proton acceptor, proton donor |
| B | GLU341 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| C | ASN55 | electrostatic stabiliser |
| C | LYS182 | electrostatic stabiliser |
| C | LYS184 | proton acceptor, proton donor |
| C | ASP213 | metal ligand |
| C | GLU239 | metal ligand |
| C | GLU265 | metal ligand |
| C | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| C | HIS322 | proton acceptor, proton donor |
| C | GLU341 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| D | ASN55 | electrostatic stabiliser |
| D | LYS182 | electrostatic stabiliser |
| D | LYS184 | proton acceptor, proton donor |
| D | ASP213 | metal ligand |
| D | GLU239 | metal ligand |
| D | GLU265 | metal ligand |
| D | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| D | HIS322 | proton acceptor, proton donor |
| D | GLU341 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| E | ASN55 | electrostatic stabiliser |
| E | LYS182 | electrostatic stabiliser |
| E | LYS184 | proton acceptor, proton donor |
| E | ASP213 | metal ligand |
| E | GLU239 | metal ligand |
| E | GLU265 | metal ligand |
| E | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| E | HIS322 | proton acceptor, proton donor |
| E | GLU341 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| F | ASN55 | electrostatic stabiliser |
| F | LYS182 | electrostatic stabiliser |
| F | LYS184 | proton acceptor, proton donor |
| F | ASP213 | metal ligand |
| F | GLU239 | metal ligand |
| F | GLU265 | metal ligand |
| F | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| F | HIS322 | proton acceptor, proton donor |
| F | GLU341 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| G | ASN55 | electrostatic stabiliser |
| G | LYS182 | electrostatic stabiliser |
| G | LYS184 | proton acceptor, proton donor |
| G | ASP213 | metal ligand |
| G | GLU239 | metal ligand |
| G | GLU265 | metal ligand |
| G | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| G | HIS322 | proton acceptor, proton donor |
| G | GLU341 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| H | ASN55 | electrostatic stabiliser |
| H | LYS182 | electrostatic stabiliser |
| H | LYS184 | proton acceptor, proton donor |
| H | ASP213 | metal ligand |
| H | GLU239 | metal ligand |
| H | GLU265 | metal ligand |
| H | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| H | HIS322 | proton acceptor, proton donor |
| H | GLU341 | electrostatic stabiliser |
| site_id | MCSA9 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| I | ASN55 | electrostatic stabiliser |
| I | LYS182 | electrostatic stabiliser |
| I | LYS184 | proton acceptor, proton donor |
| I | ASP213 | metal ligand |
| I | GLU239 | metal ligand |
| I | GLU265 | metal ligand |
| I | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| I | HIS322 | proton acceptor, proton donor |
| I | GLU341 | electrostatic stabiliser |
| site_id | MCSA10 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| J | ASN55 | electrostatic stabiliser |
| J | LYS182 | electrostatic stabiliser |
| J | LYS184 | proton acceptor, proton donor |
| J | ASP213 | metal ligand |
| J | GLU239 | metal ligand |
| J | GLU265 | metal ligand |
| J | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| J | HIS322 | proton acceptor, proton donor |
| J | GLU341 | electrostatic stabiliser |
| site_id | MCSA11 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| K | ASN55 | electrostatic stabiliser |
| K | LYS182 | electrostatic stabiliser |
| K | LYS184 | proton acceptor, proton donor |
| K | ASP213 | metal ligand |
| K | GLU239 | metal ligand |
| K | GLU265 | metal ligand |
| K | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| K | HIS322 | proton acceptor, proton donor |
| K | GLU341 | electrostatic stabiliser |
| site_id | MCSA12 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| L | ASN55 | electrostatic stabiliser |
| L | LYS182 | electrostatic stabiliser |
| L | LYS184 | proton acceptor, proton donor |
| L | ASP213 | metal ligand |
| L | GLU239 | metal ligand |
| L | GLU265 | metal ligand |
| L | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| L | HIS322 | proton acceptor, proton donor |
| L | GLU341 | electrostatic stabiliser |
| site_id | MCSA13 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| M | ASN55 | electrostatic stabiliser |
| M | LYS182 | electrostatic stabiliser |
| M | LYS184 | proton acceptor, proton donor |
| M | ASP213 | metal ligand |
| M | GLU239 | metal ligand |
| M | GLU265 | metal ligand |
| M | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| M | HIS322 | proton acceptor, proton donor |
| M | GLU341 | electrostatic stabiliser |
| site_id | MCSA14 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| N | ASN55 | electrostatic stabiliser |
| N | LYS182 | electrostatic stabiliser |
| N | LYS184 | proton acceptor, proton donor |
| N | ASP213 | metal ligand |
| N | GLU239 | metal ligand |
| N | GLU265 | metal ligand |
| N | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| N | HIS322 | proton acceptor, proton donor |
| N | GLU341 | electrostatic stabiliser |
| site_id | MCSA15 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| O | ASN55 | electrostatic stabiliser |
| O | LYS182 | electrostatic stabiliser |
| O | LYS184 | proton acceptor, proton donor |
| O | ASP213 | metal ligand |
| O | GLU239 | metal ligand |
| O | GLU265 | metal ligand |
| O | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| O | HIS322 | proton acceptor, proton donor |
| O | GLU341 | electrostatic stabiliser |
| site_id | MCSA16 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| P | ASN55 | electrostatic stabiliser |
| P | LYS182 | electrostatic stabiliser |
| P | LYS184 | proton acceptor, proton donor |
| P | ASP213 | metal ligand |
| P | GLU239 | metal ligand |
| P | GLU265 | metal ligand |
| P | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| P | HIS322 | proton acceptor, proton donor |
| P | GLU341 | electrostatic stabiliser |
