Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1F3W

RECOMBINANT RABBIT MUSCLE PYRUVATE KINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005791cellular_componentrough endoplasmic reticulum
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0030955molecular_functionpotassium ion binding
A0032869biological_processcellular response to insulin stimulus
A0046872molecular_functionmetal ion binding
A1903672biological_processpositive regulation of sprouting angiogenesis
A2000767biological_processpositive regulation of cytoplasmic translation
B0000287molecular_functionmagnesium ion binding
B0003729molecular_functionmRNA binding
B0003824molecular_functioncatalytic activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005791cellular_componentrough endoplasmic reticulum
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0030955molecular_functionpotassium ion binding
B0032869biological_processcellular response to insulin stimulus
B0046872molecular_functionmetal ion binding
B1903672biological_processpositive regulation of sprouting angiogenesis
B2000767biological_processpositive regulation of cytoplasmic translation
C0000287molecular_functionmagnesium ion binding
C0003729molecular_functionmRNA binding
C0003824molecular_functioncatalytic activity
C0004713molecular_functionprotein tyrosine kinase activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005791cellular_componentrough endoplasmic reticulum
C0006096biological_processglycolytic process
C0006417biological_processregulation of translation
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0030955molecular_functionpotassium ion binding
C0032869biological_processcellular response to insulin stimulus
C0046872molecular_functionmetal ion binding
C1903672biological_processpositive regulation of sprouting angiogenesis
C2000767biological_processpositive regulation of cytoplasmic translation
D0000287molecular_functionmagnesium ion binding
D0003729molecular_functionmRNA binding
D0003824molecular_functioncatalytic activity
D0004713molecular_functionprotein tyrosine kinase activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005791cellular_componentrough endoplasmic reticulum
D0006096biological_processglycolytic process
D0006417biological_processregulation of translation
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0030955molecular_functionpotassium ion binding
D0032869biological_processcellular response to insulin stimulus
D0046872molecular_functionmetal ion binding
D1903672biological_processpositive regulation of sprouting angiogenesis
D2000767biological_processpositive regulation of cytoplasmic translation
E0000287molecular_functionmagnesium ion binding
E0003729molecular_functionmRNA binding
E0003824molecular_functioncatalytic activity
E0004713molecular_functionprotein tyrosine kinase activity
E0004743molecular_functionpyruvate kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005791cellular_componentrough endoplasmic reticulum
E0006096biological_processglycolytic process
E0006417biological_processregulation of translation
E0016301molecular_functionkinase activity
E0016310biological_processphosphorylation
E0030955molecular_functionpotassium ion binding
E0032869biological_processcellular response to insulin stimulus
E0046872molecular_functionmetal ion binding
E1903672biological_processpositive regulation of sprouting angiogenesis
E2000767biological_processpositive regulation of cytoplasmic translation
F0000287molecular_functionmagnesium ion binding
F0003729molecular_functionmRNA binding
F0003824molecular_functioncatalytic activity
F0004713molecular_functionprotein tyrosine kinase activity
F0004743molecular_functionpyruvate kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005791cellular_componentrough endoplasmic reticulum
F0006096biological_processglycolytic process
F0006417biological_processregulation of translation
F0016301molecular_functionkinase activity
F0016310biological_processphosphorylation
F0030955molecular_functionpotassium ion binding
F0032869biological_processcellular response to insulin stimulus
F0046872molecular_functionmetal ion binding
F1903672biological_processpositive regulation of sprouting angiogenesis
F2000767biological_processpositive regulation of cytoplasmic translation
G0000287molecular_functionmagnesium ion binding
G0003729molecular_functionmRNA binding
G0003824molecular_functioncatalytic activity
G0004713molecular_functionprotein tyrosine kinase activity
G0004743molecular_functionpyruvate kinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005791cellular_componentrough endoplasmic reticulum
G0006096biological_processglycolytic process
G0006417biological_processregulation of translation
G0016301molecular_functionkinase activity
G0016310biological_processphosphorylation
G0030955molecular_functionpotassium ion binding
G0032869biological_processcellular response to insulin stimulus
G0046872molecular_functionmetal ion binding
G1903672biological_processpositive regulation of sprouting angiogenesis
G2000767biological_processpositive regulation of cytoplasmic translation
H0000287molecular_functionmagnesium ion binding
H0003729molecular_functionmRNA binding
H0003824molecular_functioncatalytic activity
H0004713molecular_functionprotein tyrosine kinase activity
H0004743molecular_functionpyruvate kinase activity
H0005515molecular_functionprotein binding
H0005524molecular_functionATP binding
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005791cellular_componentrough endoplasmic reticulum
H0006096biological_processglycolytic process
H0006417biological_processregulation of translation
H0016301molecular_functionkinase activity
H0016310biological_processphosphorylation
H0030955molecular_functionpotassium ion binding
H0032869biological_processcellular response to insulin stimulus
H0046872molecular_functionmetal ion binding
H1903672biological_processpositive regulation of sprouting angiogenesis
H2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 531
ChainResidue
AASN74
ASER76
AASP112
ATHR113

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 532
ChainResidue
AGLU271
AASP295
APYR541

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 532
ChainResidue
BASP112
BTHR113
BASN74
BSER76

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 533
ChainResidue
BGLU271
BASP295
BPYR542

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K C 533
ChainResidue
CASN74
CSER76
CASP112
CTHR113

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN C 532
ChainResidue
CGLU271
CASP295
CPYR543

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K D 534
ChainResidue
DASN74
DSER76
DASP112
DTHR113

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN D 532
ChainResidue
DGLU271
DASP295
DPYR544

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K E 535
ChainResidue
EASN74
ESER76
EASP112
ETHR113

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN E 532
ChainResidue
EGLU271
EASP295
EPYR545

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K F 536
ChainResidue
FASN74
FSER76
FASP112
FTHR113

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN F 532
ChainResidue
FGLU271
FASP295
FPYR546

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K G 537
ChainResidue
GASN74
GSER76
GASP112
GTHR113

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN G 532
ChainResidue
GGLU271
GASP295
GPYR547

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K H 538
ChainResidue
HASN74
HSER76
HASP112
HTHR113

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN H 532
ChainResidue
HGLU271
HASP295
HPYR548

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR A 541
ChainResidue
ALYS269
AGLU271
AALA292
AGLY294
AASP295
ATHR327
AMET359
AMN532

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR B 542
ChainResidue
BLYS269
BGLU271
BALA292
BGLY294
BASP295
BTHR327
BMET359
BMN533

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR C 543
ChainResidue
CLYS269
CGLU271
CALA292
CGLY294
CASP295
CTHR327
CMET359
CMN532

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR D 544
ChainResidue
DLYS269
DGLU271
DALA292
DGLY294
DASP295
DTHR327
DMET359
DMN532

site_idCC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR E 545
ChainResidue
ELYS269
EGLU271
EALA292
EGLY294
EASP295
ETHR327
EMET359
EMN532

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR F 546
ChainResidue
FGLY294
FASP295
FTHR327
FMET359
FMN532
FLYS269
FGLU271
FALA292

site_idCC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR G 547
ChainResidue
GLYS269
GGLU271
GALA292
GGLY294
GASP295
GTHR327
GMET359
GMN532

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR H 548
ChainResidue
HLYS269
HGLU271
HALA292
HGLY294
HASP295
HTHR327
HMET359
HMN532

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE264-VAL276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AVAL70
AGLU432
HPHE75
HHIS77
HPRO106
HTHR113
HLYS114
HTHR120
HGLY207
HASN272
HGLU432
HLEU464
ALEU464
HALA482
HVAL489
HPRO516
AALA482
AVAL489
APRO516
BVAL70
BPHE75
BHIS77
BPRO106
BTHR113
APHE75
BLYS114
BTHR120
BGLY207
BASN272
BGLU432
BLEU464
BALA482
BVAL489
BPRO516
CVAL70
AHIS77
CPHE75
CHIS77
CPRO106
CTHR113
CLYS114
CTHR120
CGLY207
CASN272
CGLU432
CLEU464
APRO106
CALA482
CVAL489
CPRO516
DVAL70
DPHE75
DHIS77
DPRO106
DTHR113
DLYS114
DTHR120
ATHR113
DGLY207
DASN272
DGLU432
DLEU464
DALA482
DVAL489
DPRO516
EVAL70
EPHE75
EHIS77
ALYS114
EPRO106
ETHR113
ELYS114
ETHR120
EGLY207
EASN272
EGLU432
ELEU464
EALA482
EVAL489
ATHR120
EPRO516
FVAL70
FPHE75
FHIS77
FPRO106
FTHR113
FLYS114
FTHR120
FGLY207
FASN272
AGLY207
FGLU432
FLEU464
FALA482
FVAL489
FPRO516
GVAL70
GPHE75
GHIS77
GPRO106
GTHR113
AASN272
GLYS114
GTHR120
GGLY207
GASN272
GGLU432
GLEU464
GALA482
GVAL489
GPRO516
HVAL70

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AMET73
BGLN328
CMET73
CILE270
CASP295
CLEU296
CGLN328
DMET73
DILE270
DASP295
DLEU296
AILE270
DGLN328
EMET73
EILE270
EASP295
ELEU296
EGLN328
FMET73
FILE270
FASP295
FLEU296
AASP295
FGLN328
GMET73
GILE270
GASP295
GLEU296
GGLN328
HMET73
HILE270
HASP295
HLEU296
ALEU296
HGLN328
AGLN328
BMET73
BILE270
BASP295
BLEU296

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
AILE270
BILE270
CILE270
DILE270
EILE270
FILE270
GILE270
HILE270

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11979
ChainResidueDetails
ALYS2
BLYS2
CLYS2
DLYS2
ELYS2
FLYS2
GLYS2
HLYS2

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
ASER3
BSER3
CSER3
DSER3
ESER3
FSER3
GSER3
HSER3

site_idSWS_FT_FI6
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AALA37
EGLY127
FALA37
FGLY127
GALA37
GGLY127
HALA37
HGLY127
AGLY127
BALA37
BGLY127
CALA37
CGLY127
DALA37
DGLY127
EALA37

site_idSWS_FT_FI7
Number of Residues16
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AALA41
EGLU195
FALA41
FGLU195
GALA41
GGLU195
HALA41
HGLU195
AGLU195
BALA41
BGLU195
CALA41
CGLU195
DALA41
DGLU195
EALA41

site_idSWS_FT_FI8
Number of Residues24
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AGLU62
DGLU62
DASN89
DVAL305
EGLU62
EASN89
EVAL305
FGLU62
FASN89
FVAL305
GGLU62
AASN89
GASN89
GVAL305
HGLU62
HASN89
HVAL305
AVAL305
BGLU62
BASN89
BVAL305
CGLU62
CASN89
CVAL305

site_idSWS_FT_FI9
Number of Residues16
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ASER66
EALA498
FSER66
FALA498
GSER66
GALA498
HSER66
HALA498
AALA498
BSER66
BALA498
CSER66
CALA498
DSER66
DALA498
ESER66

site_idSWS_FT_FI10
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
APHE97
EASP100
FPHE97
FASP100
GPHE97
GASP100
HPHE97
HASP100
AASP100
BPHE97
BASP100
CPHE97
CASP100
DPHE97
DASP100
EPHE97

site_idSWS_FT_FI11
Number of Residues16
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG105
EVAL175
FARG105
FVAL175
GARG105
GVAL175
HARG105
HVAL175
AVAL175
BARG105
BVAL175
CARG105
CVAL175
DARG105
DVAL175
EARG105

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AMET148
BMET148
CMET148
DMET148
EMET148
FMET148
GMET148
HMET148

site_idSWS_FT_FI13
Number of Residues16
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AVAL166
EPRO322
FVAL166
FPRO322
GVAL166
GPRO322
HVAL166
HPRO322
APRO322
BVAL166
BPRO322
CVAL166
CPRO322
DVAL166
DPRO322
EVAL166

site_idSWS_FT_FI14
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AILE266
BILE266
CILE266
DILE266
EILE266
FILE266
GILE266
HILE266

site_idSWS_FT_FI15
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AILE270
BILE270
CILE270
DILE270
EILE270
FILE270
GILE270
HILE270

site_idSWS_FT_FI16
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
AASP475
BASP475
CASP475
DASP475
EASP475
FASP475
GASP475
HASP475

site_idSWS_FT_FI17
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AGLY115
BGLY115
CGLY115
DGLY115
EGLY115
FGLY115
GGLY115
HGLY115

site_idSWS_FT_FI18
Number of Residues24
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
DILE266
DILE270
EILE266
EILE270
FILE266
FILE270
AILE266
GILE266
GILE270
HILE266
HILE270
AILE270
BILE266
BILE270
CILE266
CILE270

site_idSWS_FT_FI19
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AVAL166
BVAL166
CVAL166
DVAL166
EVAL166
FVAL166
GVAL166
HVAL166

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ALYS269
ASER361
AARG119
AGLU363
AARG72
ATHR327

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BLYS269
BSER361
BARG119
BGLU363
BARG72
BTHR327

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CLYS269
CSER361
CARG119
CGLU363
CARG72
CTHR327

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DLYS269
DSER361
DARG119
DGLU363
DARG72
DTHR327

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ELYS269
ESER361
EARG119
EGLU363
EARG72
ETHR327

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
FLYS269
FSER361
FARG119
FGLU363
FARG72
FTHR327

site_idCSA7
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
GLYS269
GSER361
GARG119
GGLU363
GARG72
GTHR327

site_idCSA8
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
HLYS269
HSER361
HARG119
HGLU363
HARG72
HTHR327

site_idMCSA1
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
AMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
ATHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
AILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
AGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA2
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
BMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
BTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
BILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
BGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA3
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
CMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
CTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
CILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
CGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA4
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
DMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
DTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
DILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
DGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA5
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
EMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
ETHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
EILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
EGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA6
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
FMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
FTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
FILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
FGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA7
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
GMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
GTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
GILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
GGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA8
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
HMET73attractive charge-charge interaction, electrostatic stabiliser, steric role
HTHR120attractive charge-charge interaction, electrostatic stabiliser, steric role
HILE270attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
HGLN328electrostatic stabiliser, hydrogen bond donor, increase acidity

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon