eF-site ID 3oo2-AB PDB Code 3oo2 Chain A, B click to enlarge Title 2.37 Angstrom resolution crystal structure of an alanine racemase (alr) from Staphylococcus aureus subsp. aureus COL Classification ISOMERASE Compound Alanine racemase 1 Source Staphylococcus aureus (strain COL) (ALR1_STAAC) Sequence A:  SDKYYRSAYMNVDLNAVASNFKVFSTLHPNKTVMAVVKAN AYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAK ILVLGVLPAKDIDKAIQHRVALTVPSKQWLKEAIKNISGE QEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLV FEGVFTHFACADEPGDMTTEQYQRFKDMVNEAIKPEYIHC QNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVHL KPSVQLIANVVQTKTLQAGESVSYGYTATDPTTIALLPIG YADGYLRIMQGSFVNVNGHQCEVIGRVCMDQTIVKVPDQV KAGDSVILIDNHRESPQSVEVVAEKQHTINYEVLCNLSRR LPRIYHDGDQRFVTNELLK B:  SDKYYRSAYMNVDLNAVASNFKVFSTLHPNKTVMAVVKAN AYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAK ILVLGVLPAKDIDKAIQHRVALTVPSKQWLKEAIKNISKK LWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGV FTHFACADEPGDMTTEQYQRFKDMVNEAIKPEYIHCQNSA GSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVHLKPSV QLIANVVQTKTLQADPTTIALLPIGYADGYLRIMQGSFVN VNGHQCEVIGRVCMDQTIVKVPDQVKAGDSVILIDNHRES PQSVEVVAEKQHTINYEVLCNLSRRLPRIYHDGDQRFVTN ELLK Description Functional site 1) chain A residue 154 type sequence I description BINDING SITE FOR RESIDUE NA A 383 source : AC1 2) chain A residue 157 type sequence Y description BINDING SITE FOR RESIDUE NA A 383 source : AC1 3) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE NA A 383 source : AC1 4) chain A residue 170 type sequence A description BINDING SITE FOR RESIDUE BME A 384 source : AC2 5) chain A residue 171 type sequence C description BINDING SITE FOR RESIDUE BME A 384 source : AC2 6) chain A residue 173 type sequence D description BINDING SITE FOR RESIDUE BME A 384 source : AC2 7) chain A residue 174 type sequence E description BINDING SITE FOR RESIDUE BME A 384 source : AC2 8) chain B residue 309 type sequence R description BINDING SITE FOR RESIDUE BME A 384 source : AC2 9) chain A residue 311 type sequence C description BINDING SITE FOR RESIDUE BME A 385 source : AC3 10) chain B residue 138 type sequence R description BINDING SITE FOR RESIDUE BME A 385 source : AC3 11) chain A residue 43 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 12) chain A residue 203 type sequence N description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 13) chain A residue 204 type sequence S description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 14) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 15) chain A residue 222 type sequence I description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 16) chain A residue 354 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 386 source : AC4 17) chain B residue 154 type sequence I description BINDING SITE FOR RESIDUE NA B 383 source : AC5 18) chain B residue 157 type sequence Y description BINDING SITE FOR RESIDUE NA B 383 source : AC5 19) chain B residue 160 type sequence L description BINDING SITE FOR RESIDUE NA B 383 source : AC5 20) chain B residue 309 type sequence R description BINDING SITE FOR RESIDUE BME B 384 source : AC6 21) chain B residue 311 type sequence C description BINDING SITE FOR RESIDUE BME B 384 source : AC6 22) chain B residue 43 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 23) chain B residue 203 type sequence N description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 24) chain B residue 204 type sequence S description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 25) chain B residue 221 type sequence G description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 26) chain B residue 222 type sequence I description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 27) chain B residue 354 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 385 source : AC7 28) chain A residue 36-46 type prosite sequence AVVKANAYGLG description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGLG source prosite : PS00395 29) chain A residue 39 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 39 type ACT_SITE sequence K description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 265 type ACT_SITE sequence Y description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 138 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 312 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 138 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 312 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 39 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 39 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01201 source Swiss-Prot : SWS_FT_FI4

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