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

2A19

PKR kinase domain- eIF2alpha- AMP-PNP complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003743molecular_functiontranslation initiation factor activity
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 1641
ChainResidue
BASP432
BANP1640

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 1642
ChainResidue
BASN419
BASP432
BANP1640

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 2642
ChainResidue
CASN419
CASP432
CANP2640
CMG2641

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 2641
ChainResidue
CASP414
CASP432
CANP2640
CMG2642

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 C 901
ChainResidue
CLYS304
CARG307
CARG413

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ANP B 1640
ChainResidue
BGLY279
BVAL281
BVAL294
BLYS296
BMET366
BGLU367
BCYS369
BSER418
BASN419
BPHE421
BASP432
BMG1641
BMG1642

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ANP C 2640
ChainResidue
CHOH36
CILE273
CGLY274
CVAL294
CGLU367
CPHE368
CCYS369
CPHE421
CMG2641
CMG2642

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGQVFkAkhridgkt..........YVIK
ChainResidueDetails
BILE273-LYS296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
BGLN427
CGLN427

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE273
CILE273

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
BLYS296
CLYS296

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:16179258, ECO:0000305|PubMed:31246429
ChainResidueDetails
BARG445
CARG445

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000305|PubMed:11152499
ChainResidueDetails
BTHR258
CTHR258

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16373505
ChainResidueDetails
BTYR293
CTYR293

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11337501, ECO:0000269|PubMed:16179258
ChainResidueDetails
BGLN459
CGLN459

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11337501, ECO:0000269|PubMed:20685959
ChainResidueDetails
BASP464
CASP464

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BVAL469
CVAL469

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP414
BSER418

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP414
CSER418

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP414
BLYS416

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP414
CLYS416

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP414
BLYS416
BTHR451

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN419
BASP414
BLYS416

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN419
CASP414
CLYS416

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon