1AQF
PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| A | 0004743 | molecular_function | pyruvate kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| B | 0004743 | molecular_function | pyruvate kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005791 | cellular_component | rough endoplasmic reticulum |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003729 | molecular_function | mRNA binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| C | 0004743 | molecular_function | pyruvate kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005791 | cellular_component | rough endoplasmic reticulum |
| C | 0006096 | biological_process | glycolytic process |
| C | 0006417 | biological_process | regulation of translation |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| C | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003729 | molecular_function | mRNA binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| D | 0004743 | molecular_function | pyruvate kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005791 | cellular_component | rough endoplasmic reticulum |
| D | 0006096 | biological_process | glycolytic process |
| D | 0006417 | biological_process | regulation of translation |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| D | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003729 | molecular_function | mRNA binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0004713 | molecular_function | protein tyrosine kinase activity |
| E | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| E | 0004743 | molecular_function | pyruvate kinase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005791 | cellular_component | rough endoplasmic reticulum |
| E | 0006096 | biological_process | glycolytic process |
| E | 0006417 | biological_process | regulation of translation |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0030955 | molecular_function | potassium ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| E | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003729 | molecular_function | mRNA binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004674 | molecular_function | protein serine/threonine kinase activity |
| F | 0004713 | molecular_function | protein tyrosine kinase activity |
| F | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| F | 0004743 | molecular_function | pyruvate kinase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005791 | cellular_component | rough endoplasmic reticulum |
| F | 0006096 | biological_process | glycolytic process |
| F | 0006417 | biological_process | regulation of translation |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0030955 | molecular_function | potassium ion binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| F | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0003729 | molecular_function | mRNA binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004674 | molecular_function | protein serine/threonine kinase activity |
| G | 0004713 | molecular_function | protein tyrosine kinase activity |
| G | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| G | 0004743 | molecular_function | pyruvate kinase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005791 | cellular_component | rough endoplasmic reticulum |
| G | 0006096 | biological_process | glycolytic process |
| G | 0006417 | biological_process | regulation of translation |
| G | 0016301 | molecular_function | kinase activity |
| G | 0016740 | molecular_function | transferase activity |
| G | 0030955 | molecular_function | potassium ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| G | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0003729 | molecular_function | mRNA binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004674 | molecular_function | protein serine/threonine kinase activity |
| H | 0004713 | molecular_function | protein tyrosine kinase activity |
| H | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| H | 0004743 | molecular_function | pyruvate kinase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005634 | cellular_component | nucleus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005791 | cellular_component | rough endoplasmic reticulum |
| H | 0006096 | biological_process | glycolytic process |
| H | 0006417 | biological_process | regulation of translation |
| H | 0016301 | molecular_function | kinase activity |
| H | 0016740 | molecular_function | transferase activity |
| H | 0030955 | molecular_function | potassium ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| H | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 533 |
| Chain | Residue |
| A | ASN74 |
| A | SER76 |
| A | ASP112 |
| A | THR113 |
| A | SER242 |
| A | PEQ532 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 534 |
| Chain | Residue |
| A | GLU271 |
| A | ASP295 |
| A | PEQ532 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 533 |
| Chain | Residue |
| B | ASN74 |
| B | SER76 |
| B | ASP112 |
| B | THR113 |
| B | SER242 |
| B | PEQ532 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 534 |
| Chain | Residue |
| B | GLU271 |
| B | ASP295 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 533 |
| Chain | Residue |
| C | ASN74 |
| C | SER76 |
| C | ASP112 |
| C | THR113 |
| C | PEQ532 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 534 |
| Chain | Residue |
| C | GLU271 |
| C | ASP295 |
| C | HOH6071 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 533 |
| Chain | Residue |
| D | ASN74 |
| D | SER76 |
| D | ASP112 |
| D | THR113 |
| D | PEQ532 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 534 |
| Chain | Residue |
| D | GLU271 |
| D | ASP295 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K E 533 |
| Chain | Residue |
| E | ASN74 |
| E | SER76 |
| E | ASP112 |
| E | THR113 |
| E | PEQ532 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 534 |
| Chain | Residue |
| E | LYS114 |
| E | GLU271 |
| E | ASP295 |
| E | PEQ532 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K F 533 |
| Chain | Residue |
| F | ASN74 |
| F | SER76 |
| F | ASP112 |
| F | THR113 |
| F | LYS114 |
| F | SER242 |
| F | PEQ532 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG F 534 |
| Chain | Residue |
| F | GLU271 |
| F | ASP295 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K G 533 |
| Chain | Residue |
| G | ASN74 |
| G | SER76 |
| G | ASP112 |
| G | THR113 |
| G | PEQ532 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG G 534 |
| Chain | Residue |
| G | GLU271 |
| G | ASP295 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K H 533 |
| Chain | Residue |
| H | ASN74 |
| H | SER76 |
| H | ASP112 |
| H | THR113 |
| H | LYS114 |
| H | PEQ532 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG H 534 |
| Chain | Residue |
| H | GLU271 |
| H | ASP295 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEQ A 532 |
| Chain | Residue |
| A | ARG72 |
| A | LYS269 |
| A | GLU271 |
| A | ALA292 |
| A | GLY294 |
| A | ASP295 |
| A | THR327 |
| A | K533 |
| A | MG534 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEQ B 532 |
| Chain | Residue |
| B | ARG72 |
| B | LYS269 |
| B | MET290 |
| B | ALA292 |
| B | GLY294 |
| B | ASP295 |
| B | THR327 |
| B | K533 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEQ C 532 |
| Chain | Residue |
| C | ARG72 |
| C | LYS269 |
| C | ASP295 |
| C | THR327 |
| C | K533 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEQ D 532 |
| Chain | Residue |
| D | ARG72 |
| D | LYS269 |
| D | GLU271 |
| D | ALA292 |
| D | GLY294 |
| D | ASP295 |
| D | THR327 |
| D | K533 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEQ E 532 |
| Chain | Residue |
| E | ASP295 |
| E | THR327 |
| E | K533 |
| E | MG534 |
| E | ARG72 |
| E | ASN74 |
| E | LYS269 |
| E | ALA292 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEQ F 532 |
| Chain | Residue |
| F | ARG72 |
| F | LYS269 |
| F | ALA292 |
| F | GLY294 |
| F | ASP295 |
| F | THR327 |
| F | K533 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEQ G 532 |
| Chain | Residue |
| G | ARG72 |
| G | LYS269 |
| G | GLU271 |
| G | ALA292 |
| G | GLY294 |
| G | ASP295 |
| G | THR327 |
| G | K533 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEQ H 532 |
| Chain | Residue |
| H | ARG72 |
| H | ASP112 |
| H | LYS269 |
| H | MET290 |
| H | ALA292 |
| H | GLY294 |
| H | ASP295 |
| H | THR327 |
| H | K533 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV |
| Chain | Residue | Details |
| A | ILE264-VAL276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1792 |
| Details | Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 198 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 7 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 24 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 7 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| A | LYS269 | |
| A | SER361 | |
| A | ARG119 | |
| A | GLU363 | |
| A | ARG72 | |
| A | THR327 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| B | LYS269 | |
| B | SER361 | |
| B | ARG119 | |
| B | GLU363 | |
| B | ARG72 | |
| B | THR327 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| C | LYS269 | |
| C | SER361 | |
| C | ARG119 | |
| C | GLU363 | |
| C | ARG72 | |
| C | THR327 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| D | LYS269 | |
| D | SER361 | |
| D | ARG119 | |
| D | GLU363 | |
| D | ARG72 | |
| D | THR327 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| E | SER361 | |
| E | LYS269 | |
| E | GLU363 | |
| E | ARG72 | |
| E | THR327 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| F | LYS269 | |
| F | SER361 | |
| F | ARG119 | |
| F | GLU363 | |
| F | ARG72 | |
| F | THR327 |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| G | LYS269 | |
| G | SER361 | |
| G | ARG119 | |
| G | GLU363 | |
| G | ARG72 | |
| G | THR327 |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| H | LYS269 | |
| H | SER361 | |
| H | ARG119 | |
| H | GLU363 | |
| H | ARG72 | |
| H | THR327 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| A | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| A | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| B | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| B | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| C | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| C | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| D | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| D | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA5 |
| Number of Residues | 3 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| E | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| E | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| E | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| F | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| F | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| G | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| G | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| H | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| H | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
