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1T9H

The crystal structure of YloQ, a circularly permuted GTPase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0019843molecular_functionrRNA binding
A0042254biological_processribosome biogenesis
A0042274biological_processribosomal small subunit biogenesis
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IUM A 401
ChainResidue
AHIS-2
AHOH479
AHIS-4
AHIS-3
AHIS-1
AASN54
AIUM407
AACT417
AHOH424
AHOH436

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IUM A 402
ChainResidue
AHIS-4
AGLU105
APRO111
APRO243
AARG246
AIUM408
AACT416
AHOH419
AHOH420
AHOH465

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IUM A 403
ChainResidue
AARG246
AIUM404
AIUM406
AIUM408
AACT416
AACT418
AHOH419
AHOH422
AHOH440
AHOH463

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IUM A 404
ChainResidue
AARG30
AGLU57
AIUM403
AACT418
AHOH422
AHOH425
AHOH458

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IUM A 405
ChainResidue
AGLU53
ALYS56
AGLU57
ATYR59
AHOH425

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IUM A 406
ChainResidue
AHIS-1
AGLU53
ALYS56
AIUM403
AIUM408
AACT417
AHOH422
AHOH425
AHOH440
AHOH458
AHOH587

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IUM A 407
ChainResidue
AARG-6
AHIS-5
AHIS-4
AHIS-3
AASN54
AASP108
AIUM401
AHOH436
AHOH451
AHOH453
AHOH607

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IUM A 408
ChainResidue
AHIS-4
AHIS-1
AARG246
AIUM402
AIUM403
AIUM406
AACT417
AHOH419
AHOH420
AHOH424
AHOH440
AHOH465

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 411
ChainResidue
ACYS252
ACYS257
AHIS259
ACYS265

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 412
ChainResidue
AASP143
ATYR145
AHOH549

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 413
ChainResidue
AHIS-1
AGLU247

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 414
ChainResidue
AGLU210
AHOH658
AHOH663

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 415
ChainResidue
AGLU286
AHOH521
AHOH595

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 416
ChainResidue
AGLU105
AGLY141
ATYR142
APRO243
AIUM402
AIUM403
AACT418
AHOH419

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 417
ChainResidue
AHIS-2
AGLU53
AASN54
AIUM401
AIUM406
AIUM408
AHOH424
AHOH440
AHOH587

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 418
ChainResidue
APHE13
AGLU57
AGLY141
AIUM403
AIUM404
AACT416
AHOH422

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01820
ChainResidueDetails
ATHR116
AGLY171

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:15223319
ChainResidueDetails
ACYS252
ACYS257
ACYS265
AHIS259

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:22544754
ChainResidueDetails
ATHR166

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PDB entries from 2024-05-15

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