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2A6P

Structure Solution to 2.2 Angstrom and Functional Characterisation of the Open Reading Frame Rv3214 from Mycobacterium tuberculosis

Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 204
ChainResidue
BARG12
BHIS13
BTHR16
BSER19
BARG23
BTHR25
BGOL205
BHOH207
BHOH255

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
AARG12
AHIS13
ATHR16
ASER19
AARG23
ATHR25
AARG64
AGOL205
AHOH211
AHOH220
AHOH255

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
AARG12
AHIS13
AGLU85
ATYR88
AHIS147
AGLY148
AHIS149
ASO4204

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 205
ChainResidue
BARG12
BHIS13
BHIS24
BGLU85
BTYR88
BHIS147
BGLY148
BSO4204
BHOH207

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues13
DetailsCASPASE_HIS Caspase family histidine active site. Hms..SrdVlFVSHG
ChainResidueDetails
AHIS136-GLY148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P36136, ECO:0000305|PubMed:16672613
ChainResidueDetails
AHIS13
BHIS13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P36136
ChainResidueDetails
AGLU85
BGLU85

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P36136
ChainResidueDetails
AHIS147
BHIS147

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AHIS13
AGLU85
AARG64
AHIS147

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BHIS13
BGLU85
BARG64
BHIS147

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PDB entries from 2025-06-18

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