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

6FA1

Antibody derived (Abd-4) small molecule binding to KRAS.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
D0007165biological_processsignal transduction
D0016020cellular_componentmembrane
E0003924molecular_functionGTPase activity
E0005525molecular_functionGTP binding
E0007165biological_processsignal transduction
E0016020cellular_componentmembrane
F0003924molecular_functionGTPase activity
F0005525molecular_functionGTP binding
F0007165biological_processsignal transduction
F0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG B 201
ChainResidue
BSER17
BTHR35
BGNP202
BHOH317
BHOH337

site_idAC2
Number of Residues28
Detailsbinding site for residue GNP B 202
ChainResidue
BLYS16
BSER17
BALA18
BPHE28
BVAL29
BASP30
BGLU31
BTYR32
BPRO34
BTHR35
BGLY60
BASN116
BLYS117
BASP119
BLEU120
BSER145
BALA146
BMG201
BHOH303
BHOH317
BHOH320
BHOH337
BHOH340
BHOH365
BGLY12
BGLY13
BVAL14
BGLY15

site_idAC3
Number of Residues7
Detailsbinding site for residue D2Z B 203
ChainResidue
BLYS5
BLEU6
BASP54
BGLN70
BTYR71
BTHR74
FASP105

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 201
ChainResidue
ASER17
ATHR35
AGNP202
AHOH309
AHOH327

site_idAC5
Number of Residues29
Detailsbinding site for residue GNP A 202
ChainResidue
AGLY12
AGLY13
AVAL14
AGLY15
ALYS16
ASER17
AALA18
APHE28
AVAL29
AASP30
AGLU31
ATYR32
APRO34
ATHR35
AGLY60
AASN116
ALYS117
AASP119
ALEU120
ASER145
AALA146
AMG201
AHOH301
AHOH306
AHOH309
AHOH324
AHOH327
AHOH371
AHOH372

site_idAC6
Number of Residues9
Detailsbinding site for residue D2Z A 203
ChainResidue
AHIS61
AHIS95
ATYR96
AILE139
APRO140
AGLU162
ALYS165
BGLU31
BASP33

site_idAC7
Number of Residues5
Detailsbinding site for residue MG C 201
ChainResidue
CSER17
CTHR35
CGNP202
CHOH316
CHOH318

site_idAC8
Number of Residues27
Detailsbinding site for residue GNP C 202
ChainResidue
CTYR32
CPRO34
CTHR35
CGLY60
CASN116
CLYS117
CASP119
CLEU120
CSER145
CALA146
CMG201
CHOH316
CHOH318
CHOH323
CHOH333
CHOH350
CGLY12
CGLY13
CVAL14
CGLY15
CLYS16
CSER17
CALA18
CPHE28
CVAL29
CASP30
CGLU31

site_idAC9
Number of Residues25
Detailsbinding site for residue GNP D 201
ChainResidue
DGLY12
DGLY13
DVAL14
DGLY15
DLYS16
DSER17
DALA18
DPHE28
DVAL29
DASP30
DGLU31
DTYR32
DPRO34
DTHR35
DGLY60
DASN116
DLYS117
DASP119
DLEU120
DSER145
DALA146
DMG202
DHOH301
DHOH306
DHOH308

site_idAD1
Number of Residues5
Detailsbinding site for residue MG D 202
ChainResidue
DSER17
DTHR35
DGNP201
DHOH306
DHOH308

site_idAD2
Number of Residues5
Detailsbinding site for residue MG E 201
ChainResidue
ESER17
ETHR35
EGNP202
EHOH306
EHOH318

site_idAD3
Number of Residues25
Detailsbinding site for residue GNP E 202
ChainResidue
EGLY12
EGLY13
EVAL14
EGLY15
ELYS16
ESER17
EALA18
EPHE28
EVAL29
EASP30
EGLU31
ETYR32
EPRO34
ETHR35
EGLY60
EASN116
ELYS117
EASP119
ESER145
EALA146
EMG201
EHOH306
EHOH318
EHOH327
EHOH336

site_idAD4
Number of Residues5
Detailsbinding site for residue MG F 201
ChainResidue
FSER17
FTHR35
FGNP202
FHOH305
FHOH333

site_idAD5
Number of Residues23
Detailsbinding site for residue GNP F 202
ChainResidue
FGLY12
FGLY13
FVAL14
FGLY15
FLYS16
FSER17
FALA18
FPHE28
FVAL29
FASP30
FTYR32
FPRO34
FTHR35
FGLY60
FASN116
FLYS117
FASP119
FSER145
FALA146
FMG201
FHOH305
FHOH333
FHOH361

site_idAD6
Number of Residues4
Detailsbinding site for residue D2Z F 203
ChainResidue
FASP54
FGLN70
FTYR71
FTHR74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:22566140
ChainResidueDetails
EGLY10
DVAL29
DALA59
DASN116
FGLY10
FVAL29
FALA59
FASN116
EVAL29
EALA59
EASN116
CGLY10
CVAL29
CALA59
CASN116
DGLY10

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine; in GTPase KRas; alternate => ECO:0000269|Ref.17
ChainResidueDetails
EMET1
CMET1
DMET1
FMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in GTPase KRas, N-terminally processed => ECO:0000269|Ref.17
ChainResidueDetails
ETHR2
CTHR2
DTHR2
FTHR2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22711838
ChainResidueDetails
ELYS104
CLYS104
DLYS104
FLYS104

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL => ECO:0000269|PubMed:19744486
ChainResidueDetails
ETHR35
CTHR35
DTHR35
FTHR35

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon