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1DP2

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004792molecular_functionthiosulfate sulfurtransferase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008097molecular_function5S rRNA binding
A0016740molecular_functiontransferase activity
A0016783molecular_functionsulfurtransferase activity
A0016784molecular_function3-mercaptopyruvate sulfurtransferase activity
A0035928biological_processrRNA import into mitochondrion
A0051029biological_processrRNA transport
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LPB A 900
ChainResidue
APHE106
ATHR141
ASER142
AGLU143
AARG186
AHOH1009
AHOH1010
AHOH1012

Functional Information from PROSITE/UniProt
site_idPS00380
Number of Residues12
DetailsRHODANESE_1 Rhodanese signature 1. YlerHVPGAsfF
ChainResidueDetails
ATYR47-PHE58

site_idPS00683
Number of Residues11
DetailsRHODANESE_2 Rhodanese C-terminal signature. VaiYDGSWfEW
ChainResidueDetails
AVAL268-TRP278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Cysteine persulfide intermediate => ECO:0000255|PROSITE-ProRule:PRU00173, ECO:0000269|PubMed:711738
ChainResidueDetails
AARG248

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATYR187
AGLY250

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22076378
ChainResidueDetails
ATRP14

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24329
ChainResidueDetails
APRO38

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52196
ChainResidueDetails
AGLU136
AARG175
ASER224
AVAL237

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52196
ChainResidueDetails
ATHR163
ALYS236

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250
ChainResidueDetails
ATRP35

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rhs
ChainResidueDetails
ALYS249
AARG186
AARG248
AVAL251
ATHR252
AGLY250

site_idMCSA1
Number of Residues8
DetailsM-CSA 153
ChainResidueDetails
ATYR187electrostatic stabiliser, hydrogen bond donor
AARG248nucleofuge, nucleophile
ALYS249electrostatic stabiliser, hydrogen bond donor
AGLY250electrostatic stabiliser
AVAL251electrostatic stabiliser, hydrogen bond donor
ATHR252electrostatic stabiliser, hydrogen bond donor
AALA253electrostatic stabiliser, hydrogen bond donor
ATRP275electrostatic stabiliser

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PDB entries from 2024-11-06

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