Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ORB

ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004792molecular_functionthiosulfate-cyanide 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 Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 297
ChainResidue
AARG182
ACYS247
AARG248
ALYS249
AGLY250
AVAL251
ATHR252

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 Residues118
DetailsDomain: {"description":"Rhodanese 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues115
DetailsDomain: {"description":"Rhodanese 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsRegion: {"description":"Hinge"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00173","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"711738","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24329","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52196","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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
AARG186electrostatic stabiliser, hydrogen bond donor
ACYS247nucleofuge, nucleophile
AARG248electrostatic stabiliser, hydrogen bond donor
ALYS249electrostatic stabiliser
AGLY250electrostatic stabiliser, hydrogen bond donor
AVAL251electrostatic stabiliser, hydrogen bond donor
ATHR252electrostatic stabiliser, hydrogen bond donor
ASER274electrostatic stabiliser

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon