eF-site ID 4ear-ABC PDB Code 4ear Chain A, B, C click to enlarge Title Crystal structure of purine nucleoside phosphorylase (W16Y, W94Y, W178Y, H257W) mutant from human complexed with DADMe-ImmG and phosphate Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Purine nucleoside phosphorylase Source Homo sapiens (Human) (PNPH_HUMAN) Sequence A:  GYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDKLT QAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQG RFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLNPK FEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMS DAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFETV AECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITN KVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMASIP LPD B:  ENGYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDK LTQAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMM QGRFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLN PKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPA MSDAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFE TVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLI TNKVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMAS IPLPDKA C:  GYTYEDYKNTAEYLLSHTKHRPQVAIICGSGLGGLTDKLT QAQIFDYSEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQG RFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAGGLNPK FEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMS DAYDRTMRQRALSTYKQMGEQRELQEGTYVMVAGPSFETV AECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITN KVIMDYESLEKANXEEVLAAGKQAAQKLEQFVSILMASIP LPDKA Description (1)  Purine nucleoside phosphorylase (E.C.2.4.2.1) Functional site 1) chain A residue 33 type sequence S description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 2) chain A residue 86 type sequence H description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 3) chain A residue 88 type sequence Y description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 4) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 5) chain A residue 118 type sequence G description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 6) chain A residue 195 type sequence V description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 7) chain A residue 200 type sequence F description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 8) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 9) chain A residue 217 type sequence V description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 10) chain A residue 218 type sequence G description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 11) chain A residue 219 type sequence M description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 12) chain A residue 242 type sequence T description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 13) chain A residue 243 type sequence N description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 14) chain A residue 257 type sequence X description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 15) chain C residue 159 type sequence F description BINDING SITE FOR RESIDUE IM5 A 301 source : AC1 16) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 17) chain A residue 33 type sequence S description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 18) chain A residue 64 type sequence H description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 19) chain A residue 84 type sequence R description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 20) chain A residue 86 type sequence H description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 21) chain A residue 115 type sequence N description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 22) chain A residue 116 type sequence A description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 23) chain A residue 220 type sequence S description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 24) chain B residue 88 type sequence Y description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 25) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 26) chain B residue 117 type sequence A description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 27) chain B residue 118 type sequence G description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 28) chain B residue 195 type sequence V description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 29) chain B residue 200 type sequence F description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 30) chain B residue 201 type sequence E description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 31) chain B residue 217 type sequence V description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 32) chain B residue 218 type sequence G description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 33) chain B residue 219 type sequence M description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 34) chain B residue 242 type sequence T description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 35) chain B residue 243 type sequence N description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 36) chain B residue 257 type sequence X description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 37) chain B residue 260 type sequence V description BINDING SITE FOR RESIDUE IM5 B 301 source : AC3 38) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 39) chain B residue 33 type sequence S description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 40) chain B residue 64 type sequence H description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 41) chain B residue 84 type sequence R description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 42) chain B residue 86 type sequence H description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 43) chain B residue 115 type sequence N description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 44) chain B residue 116 type sequence A description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 45) chain B residue 220 type sequence S description BINDING SITE FOR RESIDUE PO4 B 302 source : AC4 46) chain B residue 159 type sequence F description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 47) chain C residue 33 type sequence S description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 48) chain C residue 86 type sequence H description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 49) chain C residue 88 type sequence Y description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 50) chain C residue 116 type sequence A description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 51) chain C residue 118 type sequence G description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 52) chain C residue 195 type sequence V description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 53) chain C residue 200 type sequence F description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 54) chain C residue 201 type sequence E description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 55) chain C residue 217 type sequence V description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 56) chain C residue 218 type sequence G description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 57) chain C residue 219 type sequence M description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 58) chain C residue 242 type sequence T description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 59) chain C residue 243 type sequence N description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 60) chain C residue 257 type sequence X description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 61) chain C residue 260 type sequence V description BINDING SITE FOR RESIDUE IM5 C 301 source : AC5 62) chain C residue 32 type sequence G description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 63) chain C residue 33 type sequence S description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 64) chain C residue 64 type sequence H description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 65) chain C residue 84 type sequence R description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 66) chain C residue 86 type sequence H description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 67) chain C residue 115 type sequence N description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 68) chain C residue 116 type sequence A description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 69) chain C residue 220 type sequence S description BINDING SITE FOR RESIDUE PO4 C 302 source : AC6 70) chain A residue 33 type catalytic sequence S description 17 source MCSA : MCSA1 71) chain A residue 257 type catalytic sequence X description 17 source MCSA : MCSA1 72) chain A residue 64 type catalytic sequence H description 17 source MCSA : MCSA1 73) chain A residue 86 type catalytic sequence H description 17 source MCSA : MCSA1 74) chain A residue 88 type catalytic sequence Y description 17 source MCSA : MCSA1 75) chain A residue 89 type catalytic sequence E description 17 source MCSA : MCSA1 76) chain A residue 116 type catalytic sequence A description 17 source MCSA : MCSA1 77) chain A residue 219 type catalytic sequence M description 17 source MCSA : MCSA1 78) chain A residue 220 type catalytic sequence S description 17 source MCSA : MCSA1 79) chain A residue 243 type catalytic sequence N description 17 source MCSA : MCSA1 80) chain B residue 33 type catalytic sequence S description 17 source MCSA : MCSA2 81) chain B residue 257 type catalytic sequence X description 17 source MCSA : MCSA2 82) chain B residue 64 type catalytic sequence H description 17 source MCSA : MCSA2 83) chain B residue 86 type catalytic sequence H description 17 source MCSA : MCSA2 84) chain B residue 88 type catalytic sequence Y description 17 source MCSA : MCSA2 85) chain B residue 89 type catalytic sequence E description 17 source MCSA : MCSA2 86) chain B residue 116 type catalytic sequence A description 17 source MCSA : MCSA2 87) chain B residue 219 type catalytic sequence M description 17 source MCSA : MCSA2 88) chain B residue 220 type catalytic sequence S description 17 source MCSA : MCSA2 89) chain B residue 243 type catalytic sequence N description 17 source MCSA : MCSA2 90) chain C residue 33 type catalytic sequence S description 17 source MCSA : MCSA3 91) chain C residue 257 type catalytic sequence X description 17 source MCSA : MCSA3 92) chain C residue 64 type catalytic sequence H description 17 source MCSA : MCSA3 93) chain C residue 86 type catalytic sequence H description 17 source MCSA : MCSA3 94) chain C residue 88 type catalytic sequence Y description 17 source MCSA : MCSA3 95) chain C residue 89 type catalytic sequence E description 17 source MCSA : MCSA3 96) chain C residue 116 type catalytic sequence A description 17 source MCSA : MCSA3 97) chain C residue 219 type catalytic sequence M description 17 source MCSA : MCSA3 98) chain C residue 220 type catalytic sequence S description 17 source MCSA : MCSA3 99) chain C residue 243 type catalytic sequence N description 17 source MCSA : MCSA3 100) chain A residue 79-120 type prosite sequence VMMQGRFHMYEGYPLYKVTFPVRVFHLLGVDTLVVTNAAG GL description PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypLykvTfpVrVfhllGvdt.LVvtNAaGGL source prosite : PS01240 101) chain A residue 33 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI1 102) chain B residue 33 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI1 103) chain C residue 33 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI1 104) chain A residue 64 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P55859 source Swiss-Prot : SWS_FT_FI2 105) chain B residue 64 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P55859 source Swiss-Prot : SWS_FT_FI2 106) chain C residue 64 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P55859 source Swiss-Prot : SWS_FT_FI2 107) chain A residue 84 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI3 108) chain B residue 84 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI3 109) chain C residue 84 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI3 110) chain A residue 88 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8 source Swiss-Prot : SWS_FT_FI4 111) chain B residue 88 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8 source Swiss-Prot : SWS_FT_FI4 112) chain C residue 88 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8 source Swiss-Prot : SWS_FT_FI4 113) chain A residue 116 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 114) chain C residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 115) chain C residue 220 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 116) chain C residue 243 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 117) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 118) chain A residue 220 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 119) chain A residue 243 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 120) chain B residue 116 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 121) chain B residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 122) chain B residue 220 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 123) chain B residue 243 type BINDING sequence N description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 124) chain C residue 116 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA source Swiss-Prot : SWS_FT_FI5 125) chain A residue 219 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 126) chain A residue 257 type BINDING sequence X description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 127) chain B residue 219 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 128) chain B residue 257 type BINDING sequence X description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 129) chain C residue 219 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 130) chain C residue 257 type BINDING sequence X description BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT source Swiss-Prot : SWS_FT_FI6 131) chain A residue 243 type SITE sequence N description Important for substrate specificity => ECO:0000269|PubMed:9305964 source Swiss-Prot : SWS_FT_FI7 132) chain B residue 243 type SITE sequence N description Important for substrate specificity => ECO:0000269|PubMed:9305964 source Swiss-Prot : SWS_FT_FI7 133) chain C residue 243 type SITE sequence N description Important for substrate specificity => ECO:0000269|PubMed:9305964 source Swiss-Prot : SWS_FT_FI7 134) chain A residue 251 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 135) chain B residue 251 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 136) chain C residue 251 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links