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3FMP

Crystal structure of the nucleoporin Nup214 in complex with the DEAD-box helicase Ddx19

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0003729molecular_functionmRNA binding
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005643cellular_componentnuclear pore
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006406biological_processmRNA export from nucleus
B0010494cellular_componentcytoplasmic stress granule
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0016973biological_processpoly(A)+ mRNA export from nucleus
B0070062cellular_componentextracellular exosome
D0000166molecular_functionnucleotide binding
D0003676molecular_functionnucleic acid binding
D0003723molecular_functionRNA binding
D0003724molecular_functionRNA helicase activity
D0003729molecular_functionmRNA binding
D0004386molecular_functionhelicase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0006406biological_processmRNA export from nucleus
D0010494cellular_componentcytoplasmic stress granule
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0016973biological_processpoly(A)+ mRNA export from nucleus
D0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP B 480
ChainResidue
BLEU70
BLYS144
BTHR145
BALA146
BPHE94
BPHE112
BARG114
BGLN119
BGLN139
BGLY141
BTHR142
BGLY143

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP D 480
ChainResidue
DLEU70
DPHE94
DPHE112
DARG114
DSER116
DGLN119
DGLN139
DSER140
DGLY141
DTHR142
DGLY143
DLYS144
DTHR145
DALA146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BGLN119
BSER138
BARG429
BARG432
DGLN119
DSER138
DARG429
DARG432

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895
ChainResidueDetails
BALA2
DALA2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER30
ASER421
CSER30
CSER421

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR416
CTHR416

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER430
CSER430

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER433
CSER433

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR434
ATHR437
CTHR434
CTHR437

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR439
CTHR439

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PDB entries from 2024-04-24

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