eF-site ID 4c50-AB
PDB Code 4c50
Chain A, B

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Title Crystal Structure of the Catalase-Peroxidase (KatG) D137S mutant from Mycobacterium Tuberculosis
Classification OXIDOREDUCTASE
Compound CATALASE-PEROXIDASE
Source (KATG_MYCTU)
Sequence A:  HMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDY
AAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIR
MAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPSNASLDKA
RRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFG
FGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQ
MGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAA
LIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSY
GTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELT
KSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSL
RVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVA
RYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRA
SGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVG
WEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLV
VLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESF
AVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEM
TVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDM
GITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSEL
RALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR
B:  HMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDY
AAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIR
MAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPSNASLDKA
RRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFG
FGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQ
MGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAA
LIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSY
GTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELT
KSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSL
RVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVA
RYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRA
SGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVG
WEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLV
VLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESF
AVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEM
TVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDM
GITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSEL
RALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR
Description


Functional site
1) chain A
residue 108
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI1
2) chain B
residue 108
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI1
3) chain A
residue 321
type ACT_SITE
sequence W
description Tryptophan radical intermediate => ECO:0000269|PubMed:18052167
source Swiss-Prot : SWS_FT_FI2
4) chain B
residue 321
type ACT_SITE
sequence W
description Tryptophan radical intermediate => ECO:0000269|PubMed:18052167
source Swiss-Prot : SWS_FT_FI2
5) chain A
residue 270
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:15231843, ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:24185282, ECO:0007744|PDB:1SJ2, ECO:0007744|PDB:2CCA, ECO:0007744|PDB:2CCD, ECO:0007744|PDB:4C51
source Swiss-Prot : SWS_FT_FI3
6) chain B
residue 270
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:15231843, ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:24185282, ECO:0007744|PDB:1SJ2, ECO:0007744|PDB:2CCA, ECO:0007744|PDB:2CCD, ECO:0007744|PDB:4C51
source Swiss-Prot : SWS_FT_FI3
7) chain A
residue 104
type SITE
sequence R
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI4
8) chain B
residue 104
type SITE
sequence R
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI4
9) chain A
residue 107
type CROSSLNK
sequence W
description Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI5
10) chain B
residue 107
type CROSSLNK
sequence W
description Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI5
11) chain A
residue 229
type CROSSLNK
sequence Y
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI6
12) chain A
residue 255
type CROSSLNK
sequence M
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI6
13) chain B
residue 229
type CROSSLNK
sequence Y
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI6
14) chain B
residue 255
type CROSSLNK
sequence M
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate => ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:15231843
source Swiss-Prot : SWS_FT_FI6
15) chain A
residue 262-272
type prosite
sequence TAALIVGGHTF
description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. TAALIVGGHTF
source prosite : PS00435
16) chain A
residue 99-110
type prosite
sequence GPLFIRMAWHAA
description PEROXIDASE_2 Peroxidases active site signature. GPlfIRMaWHAA
source prosite : PS00436

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