8F5T
Rabbit muscle pyruvate kinase in complex with sodium and magnesium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003729 | molecular_function | mRNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
A | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
B | 0003729 | molecular_function | mRNA binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
B | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
C | 0003729 | molecular_function | mRNA binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
C | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
D | 0003729 | molecular_function | mRNA binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
D | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
E | 0003729 | molecular_function | mRNA binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
E | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
F | 0003729 | molecular_function | mRNA binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
F | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
G | 0003729 | molecular_function | mRNA binding |
G | 0003824 | molecular_function | catalytic activity |
G | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
G | 0032869 | biological_process | cellular response to insulin stimulus |
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 | 0000287 | molecular_function | magnesium ion binding |
H | 0003729 | molecular_function | mRNA binding |
H | 0003824 | molecular_function | catalytic activity |
H | 0004713 | molecular_function | 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 | 0030955 | molecular_function | potassium ion binding |
H | 0032869 | biological_process | cellular response to insulin stimulus |
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 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 | 112 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ASN69 | |
A | ASN74 | |
A | SER76 | |
A | ARG105 | |
A | ASP112 | |
A | THR113 | |
A | ARG119 | |
A | LYS206 | |
A | GLU271 | |
A | THR431 | |
A | HIS463 | |
A | TRP481 | |
A | ARG488 | |
A | ARG515 | |
B | ASN69 | |
B | ASN74 | |
B | SER76 | |
B | ARG105 | |
B | ASP112 | |
B | THR113 | |
B | ARG119 | |
B | LYS206 | |
B | GLU271 | |
B | THR431 | |
B | HIS463 | |
B | TRP481 | |
B | ARG488 | |
B | ARG515 | |
C | ASN69 | |
C | ASN74 | |
C | SER76 | |
C | ARG105 | |
C | ASP112 | |
C | THR113 | |
C | ARG119 | |
C | LYS206 | |
C | GLU271 | |
C | THR431 | |
C | HIS463 | |
C | TRP481 | |
C | ARG488 | |
C | ARG515 | |
D | ASN69 | |
D | ASN74 | |
D | SER76 | |
D | ARG105 | |
D | ASP112 | |
D | THR113 | |
D | ARG119 | |
D | LYS206 | |
D | GLU271 | |
D | THR431 | |
D | HIS463 | |
D | TRP481 | |
D | ARG488 | |
D | ARG515 | |
E | ASN69 | |
E | ASN74 | |
E | SER76 | |
E | ARG105 | |
E | ASP112 | |
E | THR113 | |
E | ARG119 | |
E | LYS206 | |
E | GLU271 | |
E | THR431 | |
E | HIS463 | |
E | TRP481 | |
E | ARG488 | |
E | ARG515 | |
F | ASN69 | |
F | ASN74 | |
F | SER76 | |
F | ARG105 | |
F | ASP112 | |
F | THR113 | |
F | ARG119 | |
F | LYS206 | |
F | GLU271 | |
F | THR431 | |
F | HIS463 | |
F | TRP481 | |
F | ARG488 | |
F | ARG515 | |
G | ASN69 | |
G | ASN74 | |
G | SER76 | |
G | ARG105 | |
G | ASP112 | |
G | THR113 | |
G | ARG119 | |
G | LYS206 | |
G | GLU271 | |
G | THR431 | |
G | HIS463 | |
G | TRP481 | |
G | ARG488 | |
G | ARG515 | |
H | ASN69 | |
H | ASN74 | |
H | SER76 | |
H | ARG105 | |
H | ASP112 | |
H | THR113 | |
H | ARG119 | |
H | LYS206 | |
H | GLU271 | |
H | THR431 | |
H | HIS463 | |
H | TRP481 | |
H | ARG488 | |
H | ARG515 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
Chain | Residue | Details |
A | ARG72 | |
A | LYS269 | |
A | GLY294 | |
A | ASP295 | |
A | THR327 | |
B | ARG72 | |
B | LYS269 | |
B | GLY294 | |
B | ASP295 | |
B | THR327 | |
C | ARG72 | |
C | LYS269 | |
C | GLY294 | |
C | ASP295 | |
C | THR327 | |
D | ARG72 | |
D | LYS269 | |
D | GLY294 | |
D | ASP295 | |
D | THR327 | |
E | ARG72 | |
E | LYS269 | |
E | GLY294 | |
E | ASP295 | |
E | THR327 | |
F | ARG72 | |
F | LYS269 | |
F | GLY294 | |
F | ASP295 | |
F | THR327 | |
G | ARG72 | |
G | LYS269 | |
G | GLY294 | |
G | ASP295 | |
G | THR327 | |
H | ARG72 | |
H | LYS269 | |
H | GLY294 | |
H | ASP295 | |
H | THR327 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
Chain | Residue | Details |
A | LYS269 | |
B | LYS269 | |
C | LYS269 | |
D | LYS269 | |
E | LYS269 | |
F | LYS269 | |
G | LYS269 | |
H | LYS269 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11979 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
C | SER1 | |
D | SER1 | |
E | SER1 | |
F | SER1 | |
G | SER1 | |
H | SER1 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS2 | |
B | LYS2 | |
C | LYS2 | |
D | LYS2 | |
E | LYS2 | |
F | LYS2 | |
G | LYS2 | |
H | LYS2 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | SER36 | |
A | SER126 | |
B | SER36 | |
B | SER126 | |
C | SER36 | |
C | SER126 | |
D | SER36 | |
D | SER126 | |
E | SER36 | |
E | SER126 | |
F | SER36 | |
F | SER126 | |
G | SER36 | |
G | SER126 | |
H | SER36 | |
H | SER126 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | THR40 | |
A | THR194 | |
B | THR40 | |
B | THR194 | |
C | THR40 | |
C | THR194 | |
D | THR40 | |
D | THR194 | |
E | THR40 | |
E | THR194 | |
F | THR40 | |
F | THR194 | |
G | THR40 | |
G | THR194 | |
H | THR40 | |
H | THR194 |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS61 | |
A | LYS88 | |
A | LYS304 | |
B | LYS61 | |
B | LYS88 | |
B | LYS304 | |
C | LYS61 | |
C | LYS88 | |
C | LYS304 | |
D | LYS61 | |
D | LYS88 | |
D | LYS304 | |
E | LYS61 | |
E | LYS88 | |
E | LYS304 | |
F | LYS61 | |
F | LYS88 | |
F | LYS304 | |
G | LYS61 | |
G | LYS88 | |
G | LYS304 | |
H | LYS61 | |
H | LYS88 | |
H | LYS304 |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS65 | |
A | LYS497 | |
B | LYS65 | |
B | LYS497 | |
C | LYS65 | |
C | LYS497 | |
D | LYS65 | |
D | LYS497 | |
E | LYS65 | |
E | LYS497 | |
F | LYS65 | |
F | LYS497 | |
G | LYS65 | |
G | LYS497 | |
H | LYS65 | |
H | LYS497 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
Chain | Residue | Details |
A | SER96 | |
A | SER99 | |
B | SER96 | |
B | SER99 | |
C | SER96 | |
C | SER99 | |
D | SER96 | |
D | SER99 | |
E | SER96 | |
E | SER99 | |
F | SER96 | |
F | SER99 | |
G | SER96 | |
G | SER99 | |
H | SER96 | |
H | SER99 |
site_id | SWS_FT_FI11 |
Number of Residues | 16 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | TYR104 | |
A | TYR174 | |
B | TYR104 | |
B | TYR174 | |
C | TYR104 | |
C | TYR174 | |
D | TYR104 | |
D | TYR174 | |
E | TYR104 | |
E | TYR174 | |
F | TYR104 | |
F | TYR174 | |
G | TYR104 | |
G | TYR174 | |
H | TYR104 | |
H | TYR174 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | TYR147 | |
B | TYR147 | |
C | TYR147 | |
D | TYR147 | |
E | TYR147 | |
F | TYR147 | |
G | TYR147 | |
H | TYR147 |
site_id | SWS_FT_FI13 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS165 | |
A | LYS321 | |
B | LYS165 | |
B | LYS321 | |
C | LYS165 | |
C | LYS321 | |
D | LYS165 | |
D | LYS321 | |
E | LYS165 | |
E | LYS321 | |
F | LYS165 | |
F | LYS321 | |
G | LYS165 | |
G | LYS321 | |
H | LYS165 | |
H | LYS321 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS265 | |
B | LYS265 | |
C | LYS265 | |
D | LYS265 | |
E | LYS265 | |
F | LYS265 | |
G | LYS265 | |
H | LYS265 |
site_id | SWS_FT_FI15 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS269 | |
B | LYS269 | |
C | LYS269 | |
D | LYS269 | |
E | LYS269 | |
F | LYS269 | |
G | LYS269 | |
H | LYS269 |
site_id | SWS_FT_FI16 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | LYS474 | |
B | LYS474 | |
C | LYS474 | |
D | LYS474 | |
E | LYS474 | |
F | LYS474 | |
G | LYS474 | |
H | LYS474 |
site_id | SWS_FT_FI17 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS114 | |
B | LYS114 | |
C | LYS114 | |
D | LYS114 | |
E | LYS114 | |
F | LYS114 | |
G | LYS114 | |
H | LYS114 |
site_id | SWS_FT_FI18 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS265 | |
A | LYS269 | |
B | LYS265 | |
B | LYS269 | |
C | LYS265 | |
C | LYS269 | |
D | LYS265 | |
D | LYS269 | |
E | LYS265 | |
E | LYS269 | |
F | LYS265 | |
F | LYS269 | |
G | LYS265 | |
G | LYS269 | |
H | LYS265 | |
H | LYS269 |
site_id | SWS_FT_FI19 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | LYS165 | |
B | LYS165 | |
C | LYS165 | |
D | LYS165 | |
E | LYS165 | |
F | LYS165 | |
G | LYS165 | |
H | LYS165 |
Catalytic Information from CSA
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 | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
E | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
E | ARG119 | 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 |