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1BEH

HUMAN PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN IN COMPLEX WITH CACODYLATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0008429molecular_functionphosphatidylethanolamine binding
A0019899molecular_functionenzyme binding
A0019901molecular_functionprotein kinase binding
A0030414molecular_functionpeptidase inhibitor activity
A0043409biological_processnegative regulation of MAPK cascade
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008289molecular_functionlipid binding
B0008429molecular_functionphosphatidylethanolamine binding
B0019899molecular_functionenzyme binding
B0019901molecular_functionprotein kinase binding
B0030414molecular_functionpeptidase inhibitor activity
B0043409biological_processnegative regulation of MAPK cascade
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAC A 188
ChainResidue
AASP70
ATRP84
AHIS86
AGLY110
APRO111
ATYR120
ATYR181

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CAC B 188
ChainResidue
BHIS86
BGLY110
BPRO111
BHIS118
BTYR120
BTYR181
BASP70
BTRP84

Functional Information from PROSITE/UniProt
site_idPS01220
Number of Residues23
DetailsPBP Phosphatidylethanolamine-binding protein family signature. YtLVlTDPDaPSrkdpkyrewhH
ChainResidueDetails
ATYR64-HIS86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ALYS7
ASER99
APHE154
BLYS7
BSER99
BPHE154

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31044
ChainResidueDetails
ALEU14
BLEU14

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO43
BPRO43

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AILE53
BILE53

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATRP55
BTRP55

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PDB entries from 2024-04-24

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